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Zinc in PDB 2h4h: SIR2 H116Y Mutant-P53 Peptide-Nad

Protein crystallography data

The structure of SIR2 H116Y Mutant-P53 Peptide-Nad, PDB code: 2h4h was solved by K.G.Hoff, J.L.Avalos, K.Sens, C.Wolberger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.99
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 42.260, 58.676, 106.846, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 23.7

Zinc Binding Sites:

The binding sites of Zinc atom in the SIR2 H116Y Mutant-P53 Peptide-Nad (pdb code 2h4h). 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 SIR2 H116Y Mutant-P53 Peptide-Nad, PDB code: 2h4h:

Zinc binding site 1 out of 1 in 2h4h

Go back to Zinc Binding Sites List in 2h4h
Zinc binding site 1 out of 1 in the SIR2 H116Y Mutant-P53 Peptide-Nad


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of SIR2 H116Y Mutant-P53 Peptide-Nad within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1001

b:32.6
occ:1.00
SG A:CYS127 2.0 33.6 1.0
SG A:CYS148 2.2 33.0 1.0
SG A:CYS124 2.3 26.3 1.0
SG A:CYS151 2.4 34.5 1.0
CB A:CYS124 2.9 26.4 1.0
CB A:CYS148 3.0 33.1 1.0
CB A:CYS127 3.4 32.1 1.0
CB A:CYS151 3.6 36.8 1.0
N A:CYS151 3.7 37.9 1.0
N A:CYS127 3.8 32.0 1.0
CA A:CYS127 4.1 32.4 1.0
CA A:CYS151 4.2 36.9 1.0
CB A:ASP150 4.2 38.7 1.0
CA A:CYS124 4.4 25.7 1.0
CA A:CYS148 4.5 33.6 1.0
CB A:LYS129 4.6 28.6 1.0
CB A:SER153 4.6 31.5 1.0
C A:ASP150 4.6 38.8 1.0
N A:SER153 4.7 32.8 1.0
C A:CYS127 4.8 32.1 1.0
C A:CYS151 4.8 36.6 1.0
N A:GLU128 4.8 32.0 1.0
CA A:ASP150 4.8 38.4 1.0
N A:ASP150 4.8 38.1 1.0
CB A:ARG126 4.8 31.9 1.0
OG A:SER153 4.9 33.3 1.0
N A:ASN152 4.9 35.9 1.0
N A:LYS129 4.9 29.1 1.0
C A:CYS124 5.0 25.6 1.0
C A:ARG126 5.0 31.9 1.0

Reference:

K.G.Hoff, J.L.Avalos, K.Sens, C.Wolberger. Insights Into the Sirtuin Mechanism From Ternary Complexes Containing Nad(+) and Acetylated Peptide. Structure V. 14 1231 2006.
ISSN: ISSN 0969-2126
PubMed: 16905097
DOI: 10.1016/J.STR.2006.06.006
Page generated: Wed Aug 20 03:16:39 2025

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