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Zinc in PDB 2h2i: The Structural Basis of Sirtuin Substrate Affinity

Protein crystallography data

The structure of The Structural Basis of Sirtuin Substrate Affinity, PDB code: 2h2i was solved by M.S.Cosgrove, C.Wolberger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 129.10 / 1.80
Space group P 4 3 2
Cell size a, b, c (Å), α, β, γ (°) 133.107, 133.107, 133.107, 90.00, 90.00, 90.00
R / Rfree (%) 18.6 / 21.3

Zinc Binding Sites:

The binding sites of Zinc atom in the The Structural Basis of Sirtuin Substrate Affinity (pdb code 2h2i). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the The Structural Basis of Sirtuin Substrate Affinity, PDB code: 2h2i:

Zinc binding site 1 out of 1 in 2h2i

Go back to Zinc Binding Sites List in 2h2i
Zinc binding site 1 out of 1 in the The Structural Basis of Sirtuin Substrate Affinity


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Structural Basis of Sirtuin Substrate Affinity within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1000

b:24.8
occ:1.00
SG A:CYS127 2.2 26.3 1.0
SG A:CYS151 2.3 25.3 1.0
SG A:CYS148 2.4 24.5 1.0
SG A:CYS124 2.4 22.9 1.0
CB A:CYS124 3.1 21.7 1.0
CB A:CYS148 3.1 26.1 1.0
CB A:CYS127 3.3 23.9 1.0
CB A:CYS151 3.6 30.3 1.0
N A:CYS127 3.8 22.0 1.0
N A:CYS151 3.9 30.4 1.0
CA A:CYS127 4.1 23.0 1.0
CA A:CYS151 4.2 29.3 1.0
CA A:CYS124 4.6 20.9 1.0
CA A:CYS148 4.6 26.2 1.0
CB A:ASP150 4.7 32.5 1.0
C A:CYS127 4.7 23.9 1.0
CB A:LYS129 4.7 24.6 1.0
CB A:SER153 4.8 26.9 1.0
C A:CYS151 4.8 29.1 1.0
N A:SER153 4.8 27.3 1.0
CB A:ARG126 4.8 23.7 1.0
C A:ASP150 4.8 32.5 1.0
N A:GLU128 4.8 23.9 1.0
N A:ASN152 4.9 28.9 1.0
C A:ARG126 4.9 22.8 1.0
N A:ASP150 4.9 32.6 1.0
O A:HOH1102 5.0 34.2 1.0
OG A:SER153 5.0 26.8 1.0

Reference:

M.S.Cosgrove, K.Bever, J.L.Avalos, S.Muhammad, X.Zhang, C.Wolberger. The Structural Basis of Sirtuin Substrate Affinity Biochemistry V. 45 7511 2006.
ISSN: ISSN 0006-2960
PubMed: 16768447
DOI: 10.1021/BI0526332
Page generated: Wed Aug 20 03:15:30 2025

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