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Nickel in PDB 1oid: 5'-Nucleotidase (E. Coli) with An Engineered Disulfide Bridge (S228C, P513C)

Enzymatic activity of 5'-Nucleotidase (E. Coli) with An Engineered Disulfide Bridge (S228C, P513C)

All present enzymatic activity of 5'-Nucleotidase (E. Coli) with An Engineered Disulfide Bridge (S228C, P513C):
3.1.3.5; 3.6.1.45;

Protein crystallography data

The structure of 5'-Nucleotidase (E. Coli) with An Engineered Disulfide Bridge (S228C, P513C), PDB code: 1oid was solved by R.Schultz-Heienbrok, T.Maier, N.Straeter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.1
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 80.496, 93.708, 82.901, 90.00, 97.71, 90.00
R / Rfree (%) 16.6 / 21.5

Nickel Binding Sites:

The binding sites of Nickel atom in the 5'-Nucleotidase (E. Coli) with An Engineered Disulfide Bridge (S228C, P513C) (pdb code 1oid). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total only one binding site of Nickel was determined in the 5'-Nucleotidase (E. Coli) with An Engineered Disulfide Bridge (S228C, P513C), PDB code: 1oid:

Nickel binding site 1 out of 1 in 1oid

Go back to Nickel Binding Sites List in 1oid
Nickel binding site 1 out of 1 in the 5'-Nucleotidase (E. Coli) with An Engineered Disulfide Bridge (S228C, P513C)


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of 5'-Nucleotidase (E. Coli) with An Engineered Disulfide Bridge (S228C, P513C) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni1551

b:66.8
occ:1.00
O A:HOH2238 2.4 46.3 1.0
ND1 A:HIS252 2.4 21.0 1.0
OD1 A:ASN116 2.4 22.9 1.0
OD2 A:ASP84 2.4 16.3 1.0
O A:HOH2114 2.9 51.0 1.0
NE2 A:HIS217 3.1 42.4 1.0
CE1 A:HIS252 3.3 30.4 1.0
CG A:ASN116 3.4 26.9 1.0
CG A:ASP84 3.4 21.8 1.0
CG A:HIS252 3.4 23.1 1.0
CE1 A:HIS217 3.5 59.2 1.0
CA A:HIS252 3.6 21.9 1.0
ND2 A:ASN116 3.7 22.0 1.0
CB A:HIS252 3.7 21.3 1.0
OD1 A:ASP84 3.8 21.4 1.0
OD2 A:ASP41 3.9 27.8 1.0
CD2 A:HIS217 4.0 50.3 1.0
ND1 A:HIS117 4.1 24.5 1.0
O A:HIS252 4.2 23.3 1.0
C A:HIS252 4.4 23.2 1.0
ND1 A:HIS217 4.4 57.4 1.0
NE2 A:HIS252 4.4 25.3 1.0
CB A:ASP84 4.5 19.6 1.0
CD2 A:HIS252 4.5 27.1 1.0
CE1 A:HIS117 4.6 20.5 1.0
N A:HIS252 4.6 19.5 1.0
CG A:HIS217 4.6 31.9 1.0
N A:ASN116 4.7 22.0 1.0
CB A:ASN116 4.7 22.5 1.0
OE1 A:GLN254 4.7 35.6 1.0

Reference:

R.Schultz-Heienbrok, T.Maier, N.Straeter. Trapping A 96 Degree Domain Rotation in Two Distinct Conformations By Engineered Disulfide Bridges Protein Sci. V. 13 1811 2004.
ISSN: ISSN 0961-8368
PubMed: 15215524
DOI: 10.1110/PS.04629604
Page generated: Fri Sep 25 07:57:38 2020
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