Nickel in PDB 7e3v: Metallo Beta-Lactamase Fold Protein (Camp Free)
Protein crystallography data
The structure of Metallo Beta-Lactamase Fold Protein (Camp Free), PDB code: 7e3v
was solved by
K.-Y.Lee,
D.-G.Kim,
B.-J.Lee,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
29.83 /
2.05
|
|
Space group
|
P 21 21 21
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
69.947,
120.807,
186.639,
90,
90,
90
|
|
R / Rfree (%)
|
23.8 /
27.7
|
Other elements in 7e3v:
The structure of Metallo Beta-Lactamase Fold Protein (Camp Free) also contains other interesting chemical elements:
Nickel Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
12;
Binding sites:
The binding sites of Nickel atom in the Metallo Beta-Lactamase Fold Protein (Camp Free)
(pdb code 7e3v). This binding sites where shown within
5.0 Angstroms radius around Nickel atom.
In total 12 binding sites of Nickel where determined in the
Metallo Beta-Lactamase Fold Protein (Camp Free), PDB code: 7e3v:
Jump to Nickel binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Nickel binding site 1 out
of 12 in 7e3v
Go back to
Nickel Binding Sites List in 7e3v
Nickel binding site 1 out
of 12 in the Metallo Beta-Lactamase Fold Protein (Camp Free)
 Mono view
 Stereo pair view
|
|
A full contact list of Nickel with other atoms in the Ni binding
site number 1 of Metallo Beta-Lactamase Fold Protein (Camp Free) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ni303
b:33.8
occ:0.50
|
ZN
|
A:ZN305
|
0.1
|
33.6
|
0.5
|
|
NE2
|
A:HIS110
|
2.2
|
24.4
|
1.0
|
|
NE2
|
A:HIS48
|
2.2
|
25.4
|
1.0
|
|
ND1
|
A:HIS50
|
2.2
|
26.0
|
1.0
|
|
OD2
|
A:ASP144
|
2.4
|
30.4
|
1.0
|
|
CD2
|
A:HIS110
|
3.0
|
25.2
|
1.0
|
|
NI
|
A:NI304
|
3.1
|
41.1
|
0.5
|
|
CD2
|
A:HIS48
|
3.1
|
25.5
|
1.0
|
|
ZN
|
A:ZN306
|
3.2
|
39.1
|
0.5
|
|
CE1
|
A:HIS50
|
3.2
|
27.7
|
1.0
|
|
CG
|
A:HIS50
|
3.2
|
27.2
|
1.0
|
|
CE1
|
A:HIS48
|
3.3
|
25.3
|
1.0
|
|
CE1
|
A:HIS110
|
3.3
|
24.8
|
1.0
|
|
CG
|
A:ASP144
|
3.4
|
27.3
|
1.0
|
|
CB
|
A:HIS50
|
3.5
|
26.9
|
1.0
|
|
CB
|
A:ASP144
|
3.8
|
26.9
|
1.0
|
|
NE2
|
A:HIS53
|
4.0
|
29.6
|
1.0
|
|
CD2
|
A:HIS53
|
4.0
|
29.3
|
1.0
|
|
CG
|
A:HIS110
|
4.2
|
24.4
|
1.0
|
|
ND1
|
A:HIS110
|
4.3
|
24.7
|
1.0
|
|
NE2
|
A:HIS50
|
4.3
|
26.1
|
1.0
|
|
CG
|
A:HIS48
|
4.3
|
24.8
|
1.0
|
|
ND1
|
A:HIS48
|
4.3
|
24.5
|
1.0
|
|
CD2
|
A:HIS50
|
4.3
|
26.8
|
1.0
|
|
OD1
|
A:ASP52
|
4.4
|
29.1
|
1.0
|
|
OD1
|
A:ASP144
|
4.5
|
30.0
|
1.0
|
|
OD2
|
A:ASP52
|
4.7
|
30.2
|
1.0
|
|
O
|
A:SER111
|
4.8
|
22.2
|
1.0
|
|
CA
|
A:HIS50
|
4.9
|
26.6
|
1.0
|
|
CG
|
A:ASP52
|
5.0
|
30.7
|
1.0
|
|
Nickel binding site 2 out
of 12 in 7e3v
Go back to
Nickel Binding Sites List in 7e3v
Nickel binding site 2 out
of 12 in the Metallo Beta-Lactamase Fold Protein (Camp Free)
 Mono view
 Stereo pair view
|
|
A full contact list of Nickel with other atoms in the Ni binding
site number 2 of Metallo Beta-Lactamase Fold Protein (Camp Free) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ni304
b:41.1
occ:0.50
|
ZN
|
A:ZN306
|
0.1
|
39.1
|
0.5
|
|
OD2
|
A:ASP144
|
2.1
|
30.4
|
1.0
|
|
NE2
|
A:HIS53
|
2.3
|
29.6
|
1.0
|
|
NE2
|
A:HIS195
|
2.3
|
27.3
|
1.0
|
|
OD2
|
A:ASP52
|
2.4
|
30.2
|
1.0
|
|
CD2
|
A:HIS53
|
3.0
|
29.3
|
1.0
|
|
CG
|
A:ASP144
|
3.0
|
27.3
|
1.0
|
|
NI
|
A:NI303
|
3.1
|
33.8
|
0.5
|
|
CD2
|
A:HIS195
|
3.1
|
26.1
|
1.0
|
|
ZN
|
A:ZN305
|
3.2
|
33.6
|
0.5
|
|
CG
|
A:ASP52
|
3.3
|
30.7
|
1.0
|
|
CE1
|
A:HIS195
|
3.3
|
25.9
|
1.0
|
|
OD1
|
A:ASP144
|
3.3
|
30.0
|
1.0
|
|
CE1
|
A:HIS53
|
3.4
|
31.6
|
1.0
|
|
OD1
|
A:ASP52
|
3.5
|
29.1
|
1.0
|
|
OE1
|
A:GLN8
|
4.0
|
33.4
|
1.0
|
|
NE2
|
A:HIS48
|
4.2
|
25.4
|
1.0
|
|
CG
|
A:HIS53
|
4.3
|
29.9
|
1.0
|
|
CG
|
A:HIS195
|
4.3
|
26.6
|
1.0
|
|
CE1
|
A:HIS48
|
4.3
|
25.3
|
1.0
|
|
ND1
|
A:HIS195
|
4.4
|
26.2
|
1.0
|
|
ND1
|
A:HIS53
|
4.4
|
30.4
|
1.0
|
|
CB
|
A:ASP144
|
4.4
|
26.9
|
1.0
|
|
CB
|
A:ASP52
|
4.6
|
29.9
|
1.0
|
|
NE2
|
A:HIS110
|
4.6
|
24.4
|
1.0
|
|
CD
|
A:GLN8
|
4.8
|
30.3
|
1.0
|
|
ND1
|
A:HIS50
|
5.0
|
26.0
|
1.0
|
|
Nickel binding site 3 out
of 12 in 7e3v
Go back to
Nickel Binding Sites List in 7e3v
Nickel binding site 3 out
of 12 in the Metallo Beta-Lactamase Fold Protein (Camp Free)
 Mono view
 Stereo pair view
|
|
A full contact list of Nickel with other atoms in the Ni binding
site number 3 of Metallo Beta-Lactamase Fold Protein (Camp Free) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Ni301
b:35.9
occ:0.50
|
ZN
|
B:ZN303
|
0.1
|
34.8
|
0.5
|
|
NE2
|
B:HIS48
|
2.2
|
28.8
|
1.0
|
|
ND1
|
B:HIS50
|
2.2
|
28.6
|
1.0
|
|
NE2
|
B:HIS110
|
2.3
|
26.7
|
1.0
|
|
OD2
|
B:ASP144
|
2.3
|
33.6
|
1.0
|
|
O
|
B:HOH431
|
2.3
|
50.7
|
1.0
|
|
NI
|
B:NI302
|
2.9
|
50.9
|
0.5
|
|
CD2
|
B:HIS48
|
3.0
|
28.2
|
1.0
|
|
ZN
|
B:ZN304
|
3.0
|
44.4
|
0.5
|
|
CD2
|
B:HIS110
|
3.1
|
25.4
|
1.0
|
|
CE1
|
B:HIS50
|
3.1
|
30.5
|
1.0
|
|
CG
|
B:HIS50
|
3.2
|
28.9
|
1.0
|
|
CE1
|
B:HIS48
|
3.3
|
29.3
|
1.0
|
|
CE1
|
B:HIS110
|
3.3
|
24.1
|
1.0
|
|
CG
|
B:ASP144
|
3.3
|
29.6
|
1.0
|
|
CB
|
B:HIS50
|
3.5
|
29.8
|
1.0
|
|
NE2
|
B:HIS53
|
3.8
|
37.7
|
1.0
|
|
CB
|
B:ASP144
|
3.9
|
28.0
|
1.0
|
|
O
|
A:HOH443
|
3.9
|
25.4
|
1.0
|
|
CD2
|
B:HIS53
|
4.0
|
36.8
|
1.0
|
|
OD1
|
B:ASP52
|
4.2
|
40.8
|
1.0
|
|
CG
|
B:HIS48
|
4.2
|
29.5
|
1.0
|
|
CG
|
B:HIS110
|
4.3
|
24.6
|
1.0
|
|
ND1
|
B:HIS48
|
4.3
|
30.3
|
1.0
|
|
NE2
|
B:HIS50
|
4.3
|
28.6
|
1.0
|
|
CD2
|
B:HIS50
|
4.3
|
28.6
|
1.0
|
|
OD1
|
B:ASP144
|
4.3
|
29.7
|
1.0
|
|
ND1
|
B:HIS110
|
4.3
|
25.0
|
1.0
|
|
OD2
|
B:ASP52
|
4.7
|
37.8
|
1.0
|
|
O
|
B:SER111
|
4.8
|
26.8
|
1.0
|
|
CE1
|
B:HIS53
|
4.8
|
38.6
|
1.0
|
|
CG
|
B:ASP52
|
4.9
|
39.3
|
1.0
|
|
CA
|
B:HIS50
|
4.9
|
31.5
|
1.0
|
|
CG
|
B:HIS53
|
5.0
|
36.5
|
1.0
|
|
NE2
|
B:HIS195
|
5.0
|
30.0
|
1.0
|
|
Nickel binding site 4 out
of 12 in 7e3v
Go back to
Nickel Binding Sites List in 7e3v
Nickel binding site 4 out
of 12 in the Metallo Beta-Lactamase Fold Protein (Camp Free)
 Mono view
 Stereo pair view
|
|
A full contact list of Nickel with other atoms in the Ni binding
site number 4 of Metallo Beta-Lactamase Fold Protein (Camp Free) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Ni302
b:50.9
occ:0.50
|
ZN
|
B:ZN304
|
0.2
|
44.4
|
0.5
|
|
OD2
|
B:ASP144
|
2.1
|
33.6
|
1.0
|
|
NE2
|
B:HIS53
|
2.4
|
37.7
|
1.0
|
|
NE2
|
B:HIS195
|
2.4
|
30.0
|
1.0
|
|
OD2
|
B:ASP52
|
2.4
|
37.8
|
1.0
|
|
O
|
B:HOH431
|
2.8
|
50.7
|
1.0
|
|
NI
|
B:NI301
|
2.9
|
35.9
|
0.5
|
|
ZN
|
B:ZN303
|
3.0
|
34.8
|
0.5
|
|
CG
|
B:ASP144
|
3.1
|
29.6
|
1.0
|
|
CG
|
B:ASP52
|
3.2
|
39.3
|
1.0
|
|
CD2
|
B:HIS53
|
3.2
|
36.8
|
1.0
|
|
CD2
|
B:HIS195
|
3.2
|
27.6
|
1.0
|
|
OD1
|
B:ASP52
|
3.3
|
40.8
|
1.0
|
|
OD1
|
B:ASP144
|
3.3
|
29.7
|
1.0
|
|
CE1
|
B:HIS195
|
3.4
|
29.4
|
1.0
|
|
CE1
|
B:HIS53
|
3.4
|
38.6
|
1.0
|
|
OE1
|
B:GLN8
|
4.0
|
38.1
|
1.0
|
|
NE2
|
B:HIS48
|
4.0
|
28.8
|
1.0
|
|
CE1
|
B:HIS48
|
4.3
|
29.3
|
1.0
|
|
CG
|
B:HIS195
|
4.4
|
28.8
|
1.0
|
|
CG
|
B:HIS53
|
4.4
|
36.5
|
1.0
|
|
CB
|
B:ASP144
|
4.5
|
28.0
|
1.0
|
|
ND1
|
B:HIS195
|
4.5
|
28.4
|
1.0
|
|
ND1
|
B:HIS53
|
4.5
|
36.4
|
1.0
|
|
NE2
|
B:HIS110
|
4.5
|
26.7
|
1.0
|
|
CB
|
B:ASP52
|
4.6
|
38.5
|
1.0
|
|
ND1
|
B:HIS50
|
4.8
|
28.6
|
1.0
|
|
CD
|
B:GLN8
|
4.8
|
36.5
|
1.0
|
|
CE1
|
B:HIS110
|
4.9
|
24.1
|
1.0
|
|
CB
|
B:HIS50
|
4.9
|
29.8
|
1.0
|
|
Nickel binding site 5 out
of 12 in 7e3v
Go back to
Nickel Binding Sites List in 7e3v
Nickel binding site 5 out
of 12 in the Metallo Beta-Lactamase Fold Protein (Camp Free)
 Mono view
 Stereo pair view
|
|
A full contact list of Nickel with other atoms in the Ni binding
site number 5 of Metallo Beta-Lactamase Fold Protein (Camp Free) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Ni301
b:35.5
occ:0.50
|
ZN
|
C:ZN303
|
0.1
|
34.7
|
0.5
|
|
NE2
|
C:HIS48
|
2.2
|
25.8
|
1.0
|
|
NE2
|
C:HIS110
|
2.3
|
27.9
|
1.0
|
|
ND1
|
C:HIS50
|
2.3
|
31.3
|
1.0
|
|
OD2
|
C:ASP144
|
2.4
|
34.8
|
1.0
|
|
CD2
|
C:HIS48
|
3.0
|
26.7
|
1.0
|
|
CD2
|
C:HIS110
|
3.1
|
29.9
|
1.0
|
|
NI
|
C:NI302
|
3.1
|
47.6
|
0.5
|
|
ZN
|
C:ZN304
|
3.2
|
44.4
|
0.5
|
|
O
|
C:HOH438
|
3.2
|
40.0
|
1.0
|
|
CG
|
C:HIS50
|
3.3
|
33.0
|
1.0
|
|
CE1
|
C:HIS50
|
3.3
|
32.1
|
1.0
|
|
CE1
|
C:HIS110
|
3.3
|
28.6
|
1.0
|
|
CE1
|
C:HIS48
|
3.3
|
26.4
|
1.0
|
|
CG
|
C:ASP144
|
3.4
|
31.5
|
1.0
|
|
CB
|
C:HIS50
|
3.5
|
31.5
|
1.0
|
|
CB
|
C:ASP144
|
3.8
|
30.9
|
1.0
|
|
NE2
|
C:HIS53
|
3.9
|
32.3
|
1.0
|
|
CD2
|
C:HIS53
|
4.0
|
34.7
|
1.0
|
|
CG
|
C:HIS48
|
4.2
|
26.5
|
1.0
|
|
CG
|
C:HIS110
|
4.3
|
28.8
|
1.0
|
|
OD1
|
C:ASP52
|
4.3
|
40.4
|
1.0
|
|
ND1
|
C:HIS48
|
4.4
|
25.6
|
1.0
|
|
ND1
|
C:HIS110
|
4.4
|
28.9
|
1.0
|
|
CD2
|
C:HIS50
|
4.4
|
31.6
|
1.0
|
|
NE2
|
C:HIS50
|
4.4
|
31.5
|
1.0
|
|
OD1
|
C:ASP144
|
4.4
|
32.4
|
1.0
|
|
O
|
C:SER111
|
4.8
|
26.8
|
1.0
|
|
OD2
|
C:ASP52
|
4.8
|
41.0
|
1.0
|
|
CE1
|
C:HIS53
|
4.9
|
33.2
|
1.0
|
|
CA
|
C:HIS50
|
4.9
|
32.6
|
1.0
|
|
Nickel binding site 6 out
of 12 in 7e3v
Go back to
Nickel Binding Sites List in 7e3v
Nickel binding site 6 out
of 12 in the Metallo Beta-Lactamase Fold Protein (Camp Free)
 Mono view
 Stereo pair view
|
|
A full contact list of Nickel with other atoms in the Ni binding
site number 6 of Metallo Beta-Lactamase Fold Protein (Camp Free) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Ni302
b:47.6
occ:0.50
|
ZN
|
C:ZN304
|
0.1
|
44.4
|
0.5
|
|
OD2
|
C:ASP144
|
2.2
|
34.8
|
1.0
|
|
NE2
|
C:HIS53
|
2.3
|
32.3
|
1.0
|
|
NE2
|
C:HIS195
|
2.3
|
29.5
|
1.0
|
|
OD2
|
C:ASP52
|
2.4
|
41.0
|
1.0
|
|
O
|
C:HOH438
|
2.7
|
40.0
|
1.0
|
|
CD2
|
C:HIS53
|
3.1
|
34.7
|
1.0
|
|
NI
|
C:NI301
|
3.1
|
35.5
|
0.5
|
|
CG
|
C:ASP144
|
3.2
|
31.5
|
1.0
|
|
CD2
|
C:HIS195
|
3.2
|
28.5
|
1.0
|
|
CG
|
C:ASP52
|
3.2
|
41.8
|
1.0
|
|
ZN
|
C:ZN303
|
3.2
|
34.7
|
0.5
|
|
CE1
|
C:HIS195
|
3.3
|
29.9
|
1.0
|
|
OD1
|
C:ASP144
|
3.4
|
32.4
|
1.0
|
|
OD1
|
C:ASP52
|
3.4
|
40.4
|
1.0
|
|
CE1
|
C:HIS53
|
3.4
|
33.2
|
1.0
|
|
OE1
|
C:GLN8
|
3.9
|
37.4
|
1.0
|
|
NE2
|
C:HIS48
|
4.1
|
25.8
|
1.0
|
|
CG
|
C:HIS53
|
4.3
|
34.4
|
1.0
|
|
CG
|
C:HIS195
|
4.3
|
30.0
|
1.0
|
|
CE1
|
C:HIS48
|
4.4
|
26.4
|
1.0
|
|
ND1
|
C:HIS195
|
4.4
|
31.1
|
1.0
|
|
ND1
|
C:HIS53
|
4.4
|
32.8
|
1.0
|
|
CB
|
C:ASP144
|
4.5
|
30.9
|
1.0
|
|
CB
|
C:ASP52
|
4.6
|
40.5
|
1.0
|
|
NE2
|
C:HIS110
|
4.7
|
27.9
|
1.0
|
|
CD
|
C:GLN8
|
4.8
|
34.8
|
1.0
|
|
Nickel binding site 7 out
of 12 in 7e3v
Go back to
Nickel Binding Sites List in 7e3v
Nickel binding site 7 out
of 12 in the Metallo Beta-Lactamase Fold Protein (Camp Free)
 Mono view
 Stereo pair view
|
|
A full contact list of Nickel with other atoms in the Ni binding
site number 7 of Metallo Beta-Lactamase Fold Protein (Camp Free) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Ni303
b:33.5
occ:0.50
|
ZN
|
D:ZN305
|
0.1
|
32.9
|
0.5
|
|
NE2
|
D:HIS48
|
2.2
|
21.7
|
1.0
|
|
NE2
|
D:HIS110
|
2.2
|
26.8
|
1.0
|
|
ND1
|
D:HIS50
|
2.2
|
27.5
|
1.0
|
|
OD2
|
D:ASP144
|
2.4
|
30.2
|
1.0
|
|
CD2
|
D:HIS48
|
3.0
|
25.6
|
1.0
|
|
NI
|
D:NI304
|
3.1
|
44.9
|
0.5
|
|
ZN
|
D:ZN306
|
3.1
|
42.8
|
0.5
|
|
CD2
|
D:HIS110
|
3.1
|
24.9
|
1.0
|
|
CE1
|
D:HIS50
|
3.2
|
27.0
|
1.0
|
|
CG
|
D:HIS50
|
3.2
|
28.5
|
1.0
|
|
CE1
|
D:HIS110
|
3.2
|
26.1
|
1.0
|
|
CE1
|
D:HIS48
|
3.3
|
23.2
|
1.0
|
|
O
|
D:HOH441
|
3.4
|
36.2
|
1.0
|
|
CG
|
D:ASP144
|
3.4
|
27.8
|
1.0
|
|
CB
|
D:HIS50
|
3.4
|
29.1
|
1.0
|
|
CB
|
D:ASP144
|
3.9
|
26.6
|
1.0
|
|
NE2
|
D:HIS53
|
3.9
|
31.7
|
1.0
|
|
O
|
F:HOH431
|
4.0
|
29.3
|
1.0
|
|
CD2
|
D:HIS53
|
4.0
|
31.9
|
1.0
|
|
CG
|
D:HIS48
|
4.2
|
25.6
|
1.0
|
|
CG
|
D:HIS110
|
4.3
|
23.9
|
1.0
|
|
ND1
|
D:HIS110
|
4.3
|
23.4
|
1.0
|
|
ND1
|
D:HIS48
|
4.3
|
23.6
|
1.0
|
|
NE2
|
D:HIS50
|
4.3
|
27.2
|
1.0
|
|
CD2
|
D:HIS50
|
4.3
|
27.6
|
1.0
|
|
OD1
|
D:ASP52
|
4.4
|
36.3
|
1.0
|
|
OD1
|
D:ASP144
|
4.4
|
27.0
|
1.0
|
|
OD2
|
D:ASP52
|
4.8
|
37.0
|
1.0
|
|
O
|
D:SER111
|
4.9
|
24.0
|
1.0
|
|
CE1
|
D:HIS53
|
4.9
|
31.4
|
1.0
|
|
CA
|
D:HIS50
|
4.9
|
30.4
|
1.0
|
|
Nickel binding site 8 out
of 12 in 7e3v
Go back to
Nickel Binding Sites List in 7e3v
Nickel binding site 8 out
of 12 in the Metallo Beta-Lactamase Fold Protein (Camp Free)
 Mono view
 Stereo pair view
|
|
A full contact list of Nickel with other atoms in the Ni binding
site number 8 of Metallo Beta-Lactamase Fold Protein (Camp Free) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Ni304
b:44.9
occ:0.50
|
ZN
|
D:ZN306
|
0.1
|
42.8
|
0.5
|
|
OD2
|
D:ASP144
|
2.2
|
30.2
|
1.0
|
|
NE2
|
D:HIS53
|
2.3
|
31.7
|
1.0
|
|
NE2
|
D:HIS195
|
2.3
|
28.5
|
1.0
|
|
OD2
|
D:ASP52
|
2.4
|
37.0
|
1.0
|
|
O
|
D:HOH441
|
2.6
|
36.2
|
1.0
|
|
NI
|
D:NI303
|
3.1
|
33.5
|
0.5
|
|
CD2
|
D:HIS53
|
3.1
|
31.9
|
1.0
|
|
CG
|
D:ASP144
|
3.1
|
27.8
|
1.0
|
|
ZN
|
D:ZN305
|
3.1
|
32.9
|
0.5
|
|
CD2
|
D:HIS195
|
3.2
|
27.7
|
1.0
|
|
CG
|
D:ASP52
|
3.2
|
37.0
|
1.0
|
|
CE1
|
D:HIS53
|
3.4
|
31.4
|
1.0
|
|
OD1
|
D:ASP144
|
3.4
|
27.0
|
1.0
|
|
CE1
|
D:HIS195
|
3.4
|
28.7
|
1.0
|
|
OD1
|
D:ASP52
|
3.4
|
36.3
|
1.0
|
|
OE1
|
D:GLN8
|
4.0
|
34.2
|
1.0
|
|
NE2
|
D:HIS48
|
4.0
|
21.7
|
1.0
|
|
CE1
|
D:HIS48
|
4.3
|
23.2
|
1.0
|
|
CG
|
D:HIS53
|
4.3
|
32.0
|
1.0
|
|
CG
|
D:HIS195
|
4.4
|
28.9
|
1.0
|
|
ND1
|
D:HIS53
|
4.4
|
31.6
|
1.0
|
|
ND1
|
D:HIS195
|
4.5
|
28.8
|
1.0
|
|
CB
|
D:ASP144
|
4.5
|
26.6
|
1.0
|
|
CB
|
D:ASP52
|
4.6
|
36.7
|
1.0
|
|
NE2
|
D:HIS110
|
4.7
|
26.8
|
1.0
|
|
CD
|
D:GLN8
|
4.8
|
33.0
|
1.0
|
|
ND1
|
D:HIS50
|
5.0
|
27.5
|
1.0
|
|
Nickel binding site 9 out
of 12 in 7e3v
Go back to
Nickel Binding Sites List in 7e3v
Nickel binding site 9 out
of 12 in the Metallo Beta-Lactamase Fold Protein (Camp Free)
 Mono view
 Stereo pair view
|
|
A full contact list of Nickel with other atoms in the Ni binding
site number 9 of Metallo Beta-Lactamase Fold Protein (Camp Free) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Ni301
b:34.1
occ:0.50
|
ZN
|
E:ZN303
|
0.1
|
33.6
|
0.5
|
|
NE2
|
E:HIS110
|
2.1
|
24.2
|
1.0
|
|
NE2
|
E:HIS48
|
2.2
|
21.8
|
1.0
|
|
ND1
|
E:HIS50
|
2.3
|
28.8
|
1.0
|
|
OD2
|
E:ASP144
|
2.5
|
30.4
|
1.0
|
|
CD2
|
E:HIS110
|
3.0
|
24.2
|
1.0
|
|
CE1
|
E:HIS110
|
3.1
|
25.9
|
1.0
|
|
NI
|
E:NI302
|
3.1
|
38.0
|
0.5
|
|
CD2
|
E:HIS48
|
3.2
|
22.7
|
1.0
|
|
CE1
|
E:HIS48
|
3.2
|
24.2
|
1.0
|
|
ZN
|
E:ZN304
|
3.2
|
36.8
|
0.5
|
|
CG
|
E:HIS50
|
3.3
|
29.4
|
1.0
|
|
CE1
|
E:HIS50
|
3.3
|
30.4
|
1.0
|
|
CG
|
E:ASP144
|
3.4
|
28.6
|
1.0
|
|
CB
|
E:HIS50
|
3.5
|
29.8
|
1.0
|
|
CB
|
E:ASP144
|
3.8
|
26.6
|
1.0
|
|
O
|
D:HOH438
|
3.9
|
31.7
|
1.0
|
|
NE2
|
E:HIS53
|
4.1
|
27.3
|
1.0
|
|
CD2
|
E:HIS53
|
4.2
|
27.4
|
1.0
|
|
ND1
|
E:HIS110
|
4.2
|
25.3
|
1.0
|
|
CG
|
E:HIS110
|
4.2
|
24.1
|
1.0
|
|
ND1
|
E:HIS48
|
4.3
|
23.3
|
1.0
|
|
CG
|
E:HIS48
|
4.3
|
23.0
|
1.0
|
|
OD1
|
E:ASP52
|
4.4
|
31.7
|
1.0
|
|
CD2
|
E:HIS50
|
4.4
|
28.7
|
1.0
|
|
NE2
|
E:HIS50
|
4.4
|
28.8
|
1.0
|
|
OD1
|
E:ASP144
|
4.5
|
29.5
|
1.0
|
|
O
|
E:SER111
|
4.7
|
23.6
|
1.0
|
|
OD2
|
E:ASP52
|
4.8
|
31.6
|
1.0
|
|
CA
|
E:HIS50
|
4.9
|
27.8
|
1.0
|
|
Nickel binding site 10 out
of 12 in 7e3v
Go back to
Nickel Binding Sites List in 7e3v
Nickel binding site 10 out
of 12 in the Metallo Beta-Lactamase Fold Protein (Camp Free)
 Mono view
 Stereo pair view
|
|
A full contact list of Nickel with other atoms in the Ni binding
site number 10 of Metallo Beta-Lactamase Fold Protein (Camp Free) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Ni302
b:38.0
occ:0.50
|
ZN
|
E:ZN304
|
0.1
|
36.8
|
0.5
|
|
OD2
|
E:ASP144
|
2.1
|
30.4
|
1.0
|
|
NE2
|
E:HIS195
|
2.2
|
27.2
|
1.0
|
|
NE2
|
E:HIS53
|
2.3
|
27.3
|
1.0
|
|
OD2
|
E:ASP52
|
2.4
|
31.6
|
1.0
|
|
CG
|
E:ASP144
|
3.1
|
28.6
|
1.0
|
|
CD2
|
E:HIS195
|
3.1
|
25.3
|
1.0
|
|
CD2
|
E:HIS53
|
3.1
|
27.4
|
1.0
|
|
NI
|
E:NI301
|
3.1
|
34.1
|
0.5
|
|
ZN
|
E:ZN303
|
3.2
|
33.6
|
0.5
|
|
CG
|
E:ASP52
|
3.2
|
31.8
|
1.0
|
|
CE1
|
E:HIS195
|
3.3
|
26.1
|
1.0
|
|
OD1
|
E:ASP144
|
3.4
|
29.5
|
1.0
|
|
CE1
|
E:HIS53
|
3.4
|
27.4
|
1.0
|
|
OD1
|
E:ASP52
|
3.5
|
31.7
|
1.0
|
|
OE1
|
E:GLN8
|
4.1
|
33.7
|
1.0
|
|
NE2
|
E:HIS48
|
4.3
|
21.8
|
1.0
|
|
CG
|
E:HIS195
|
4.3
|
26.0
|
1.0
|
|
ND1
|
E:HIS195
|
4.3
|
26.1
|
1.0
|
|
CE1
|
E:HIS48
|
4.3
|
24.2
|
1.0
|
|
CG
|
E:HIS53
|
4.3
|
27.3
|
1.0
|
|
ND1
|
E:HIS53
|
4.4
|
26.3
|
1.0
|
|
CB
|
E:ASP144
|
4.4
|
26.6
|
1.0
|
|
CB
|
E:ASP52
|
4.6
|
31.4
|
1.0
|
|
NE2
|
E:HIS110
|
4.6
|
24.2
|
1.0
|
|
CD
|
E:GLN8
|
4.9
|
29.3
|
1.0
|
|
CE1
|
E:HIS110
|
4.9
|
25.9
|
1.0
|
|
Reference:
K.-Y.Lee,
D.-G.Kim,
B.-J.Lee.
Metallo Beta-Lactamase Fold Protein To Be Published.
Page generated: Fri Apr 7 19:06:06 2023
|
