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Zinc in PDB 1sdz: Crystal Structure of DIAP1 BIR1 Bound to A Reaper Peptide

Protein crystallography data

The structure of Crystal Structure of DIAP1 BIR1 Bound to A Reaper Peptide, PDB code: 1sdz was solved by N.Yan, J.W.Wu, Y.Shi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.78
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 84.800, 84.800, 49.800, 90.00, 90.00, 120.00
R / Rfree (%) 23.2 / 26.7

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of DIAP1 BIR1 Bound to A Reaper Peptide (pdb code 1sdz). 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 Crystal Structure of DIAP1 BIR1 Bound to A Reaper Peptide, PDB code: 1sdz:

Zinc binding site 1 out of 1 in 1sdz

Go back to Zinc Binding Sites List in 1sdz
Zinc binding site 1 out of 1 in the Crystal Structure of DIAP1 BIR1 Bound to A Reaper Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of DIAP1 BIR1 Bound to A Reaper Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn155

b:27.6
occ:1.00
SG A:CYS80 2.1 26.4 1.0
SG A:CYS107 2.2 31.5 1.0
NE2 A:HIS100 2.3 30.4 1.0
SG A:CYS83 2.4 27.9 1.0
CE1 A:HIS100 2.9 28.1 1.0
CB A:CYS80 3.1 28.5 1.0
CB A:CYS107 3.1 30.2 1.0
CB A:CYS83 3.2 31.1 1.0
O A:HOH229 3.4 94.8 1.0
CD2 A:HIS100 3.5 26.7 1.0
N A:CYS83 3.7 33.2 1.0
CA A:CYS83 4.1 30.3 1.0
ND1 A:HIS100 4.2 26.1 1.0
CA A:CYS107 4.4 32.1 1.0
CG A:HIS100 4.5 28.4 1.0
CG1 A:VAL85 4.5 29.0 1.0
CA A:CYS80 4.5 29.1 1.0
C A:PHE82 4.6 34.7 1.0
OG A:SER104 4.6 30.2 1.0
CB A:PHE82 4.7 33.4 1.0
C A:CYS83 4.9 30.9 1.0
CB A:SER104 4.9 32.4 1.0
N A:GLY84 4.9 30.9 1.0
N A:PHE82 4.9 33.7 1.0
CA A:PHE82 4.9 34.4 1.0

Reference:

N.Yan, J.W.Wu, J.Chai, W.Li, Y.Shi. Molecular Mechanisms of Drice Inhibition By DIAP1 and Removal of Inhibition By Reaper, Hid and Grim. Nat.Struct.Mol.Biol. V. 11 420 2004.
ISSN: ISSN 1545-9993
PubMed: 15107838
DOI: 10.1038/NSMB764
Page generated: Tue Aug 19 23:07:07 2025

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