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Nickel in PDB 2arp: Activin A in Complex with FS12 Fragment of Follistatin

Protein crystallography data

The structure of Activin A in Complex with FS12 Fragment of Follistatin, PDB code: 2arp was solved by A.E.Harrington, S.A.Morris-Triggs, B.T.Ruotolo, C.V.Robinson, S.Ohnuma, M.Hyvonen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.80 / 2.00
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 79.297, 94.502, 44.873, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 25.4

Nickel Binding Sites:

The binding sites of Nickel atom in the Activin A in Complex with FS12 Fragment of Follistatin (pdb code 2arp). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total 3 binding sites of Nickel where determined in the Activin A in Complex with FS12 Fragment of Follistatin, PDB code: 2arp:
Jump to Nickel binding site number: 1; 2; 3;

Nickel binding site 1 out of 3 in 2arp

Go back to Nickel Binding Sites List in 2arp
Nickel binding site 1 out of 3 in the Activin A in Complex with FS12 Fragment of Follistatin


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Activin A in Complex with FS12 Fragment of Follistatin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni501

b:37.5
occ:1.00
O A:HOH566 1.7 32.1 1.0
NE2 A:HIS65 2.0 36.4 1.0
NE2 A:HIS71 2.1 38.2 1.0
O A:HOH523 2.1 38.2 1.0
O A:HOH514 2.2 33.9 1.0
O A:HOH512 2.5 48.0 1.0
CE1 A:HIS65 2.8 36.0 1.0
CD2 A:HIS71 3.0 35.4 1.0
CE1 A:HIS71 3.1 36.0 1.0
CD2 A:HIS65 3.1 37.5 1.0
ND1 A:HIS65 4.0 35.0 1.0
CG A:HIS65 4.2 35.8 1.0
ND1 A:HIS71 4.2 34.1 1.0
CG A:HIS71 4.2 36.1 1.0
CE A:MET68 4.4 30.0 0.3
CE A:MET68 4.5 47.1 0.7
O A:HIS65 4.9 31.0 1.0

Nickel binding site 2 out of 3 in 2arp

Go back to Nickel Binding Sites List in 2arp
Nickel binding site 2 out of 3 in the Activin A in Complex with FS12 Fragment of Follistatin


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 2 of Activin A in Complex with FS12 Fragment of Follistatin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni502

b:36.8
occ:1.00
O F:HOH357 2.0 28.0 1.0
O F:HOH375 2.0 33.1 1.0
ND1 A:HIS36 2.0 30.3 1.0
OE2 F:GLU126 2.3 33.6 1.0
OE1 F:GLU126 2.4 31.8 1.0
O A:HOH540 2.5 34.8 1.0
CD F:GLU126 2.6 31.1 1.0
CE1 A:HIS36 2.8 28.6 1.0
CG A:HIS36 3.2 28.4 1.0
CB A:HIS36 3.7 28.1 1.0
N A:HIS36 3.7 26.8 1.0
O F:HOH342 4.0 32.7 1.0
NE2 A:HIS36 4.0 29.7 1.0
CG F:GLU126 4.1 28.5 1.0
O2 F:GOL302 4.2 56.9 1.0
CD2 A:HIS36 4.2 30.0 1.0
CA A:HIS36 4.3 27.3 1.0
O A:HOH506 4.5 35.8 1.0
C A:TYR35 4.6 24.7 1.0
O A:HOH544 4.6 25.7 1.0
CA A:TYR35 4.6 26.5 1.0
CD1 A:PHE17 4.8 29.5 1.0
NH2 F:ARG120 4.9 40.0 1.0
CB F:GLU126 5.0 28.5 1.0

Nickel binding site 3 out of 3 in 2arp

Go back to Nickel Binding Sites List in 2arp
Nickel binding site 3 out of 3 in the Activin A in Complex with FS12 Fragment of Follistatin


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 3 of Activin A in Complex with FS12 Fragment of Follistatin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni503

b:80.8
occ:1.00
O A:HOH565 2.5 54.5 1.0
NZ A:LYS13 2.7 50.3 1.0
O A:HOH563 3.3 56.3 1.0
CE A:LYS13 3.4 48.7 1.0
O A:HOH564 3.6 54.1 1.0
O A:GLU111 3.9 38.1 1.0
OE2 A:GLU111 4.2 49.9 1.0
OE1 A:GLU3 4.3 70.7 1.0
CD A:LYS13 4.7 47.9 1.0
CD A:GLU111 4.8 47.6 1.0
NZ F:LYS75 4.9 57.8 1.0
CB A:LEU2 5.0 71.5 1.0

Reference:

A.E.Harrington, S.A.Morris-Triggs, B.T.Ruotolo, C.V.Robinson, S.Ohnuma, M.Hyvonen. Structural Basis For the Inhibition of Activin Signalling By Follistatin Embo J. V. 25 1035 2006.
ISSN: ISSN 0261-4189
PubMed: 16482217
DOI: 10.1038/SJ.EMBOJ.7601000
Page generated: Wed Oct 9 16:37:49 2024

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