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Zinc in PDB 1gpc: Core GP32, Dna-Binding Protein

Protein crystallography data

The structure of Core GP32, Dna-Binding Protein, PDB code: 1gpc was solved by Y.Shamoo, A.M.Friedman, M.R.Parsons, W.H.Konigsberg, T.A.Steitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.20
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 66.500, 66.500, 235.400, 90.00, 90.00, 120.00
R / Rfree (%) 23.6 / n/a

Zinc Binding Sites:

The binding sites of Zinc atom in the Core GP32, Dna-Binding Protein (pdb code 1gpc). 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 Core GP32, Dna-Binding Protein, PDB code: 1gpc:

Zinc binding site 1 out of 1 in 1gpc

Go back to Zinc Binding Sites List in 1gpc
Zinc binding site 1 out of 1 in the Core GP32, Dna-Binding Protein


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Core GP32, Dna-Binding Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1

b:27.1
occ:1.00
SG A:CYS87 2.1 21.6 1.0
SG A:CYS90 2.2 27.3 1.0
SG A:CYS77 2.2 28.0 1.0
HE2 A:HIS64 2.4 0.0 1.0
NE2 A:HIS64 2.7 22.9 1.0
CD2 A:HIS64 3.1 23.6 1.0
CB A:CYS87 3.2 23.6 1.0
CB A:CYS90 3.3 29.5 1.0
CB A:CYS77 3.4 23.1 1.0
H A:CYS90 3.5 0.0 1.0
N A:CYS90 3.7 28.2 1.0
CA A:CYS90 3.9 28.0 1.0
CE1 A:HIS64 3.9 0.0 1.0
H A:SER79 4.3 0.0 1.0
CA A:CYS77 4.3 23.8 1.0
O A:HOH264 4.4 19.7 1.0
CG A:HIS64 4.4 25.4 1.0
C A:VAL89 4.5 25.7 1.0
H A:SER78 4.5 0.0 1.0
CA A:CYS87 4.5 26.7 1.0
O A:CYS87 4.6 29.0 1.0
CB A:VAL89 4.7 21.8 1.0
H A:VAL89 4.7 0.0 1.0
ND1 A:HIS64 4.7 26.5 1.0
C A:CYS87 4.8 26.5 1.0
CB A:ARG111 4.9 24.4 1.0
OG A:SER79 4.9 31.5 1.0
CB A:SER79 4.9 28.7 1.0
CA A:VAL89 5.0 22.4 1.0
H1 A:HOH264 5.0 0.0 1.0
N A:SER78 5.0 26.2 1.0

Reference:

Y.Shamoo, A.M.Friedman, M.R.Parsons, W.H.Konigsberg, T.A.Steitz. Crystal Structure of A Replication Fork Single-Stranded Dna Binding Protein (T4 GP32) Complexed to Dna. Nature V. 376 362 1995.
ISSN: ISSN 0028-0836
PubMed: 7630406
DOI: 10.1038/376362A0
Page generated: Wed Dec 16 02:50:17 2020

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