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Zinc in PDB 5zb1: Monomeric Crystal Structure of ORF57 From Kshv

Protein crystallography data

The structure of Monomeric Crystal Structure of ORF57 From Kshv, PDB code: 5zb1 was solved by Z.Q.Gao, F.Yuan, K.Lan, Y.H.Dong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.98 / 3.06
Space group I 4 3 2
Cell size a, b, c (Å), α, β, γ (°) 175.782, 175.782, 175.782, 90.00, 90.00, 90.00
R / Rfree (%) 22.3 / 26.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Monomeric Crystal Structure of ORF57 From Kshv (pdb code 5zb1). 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 Monomeric Crystal Structure of ORF57 From Kshv, PDB code: 5zb1:

Zinc binding site 1 out of 1 in 5zb1

Go back to Zinc Binding Sites List in 5zb1
Zinc binding site 1 out of 1 in the Monomeric Crystal Structure of ORF57 From Kshv


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Monomeric Crystal Structure of ORF57 From Kshv within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn500

b:85.8
occ:1.00
SG A:CYS432 2.0 79.6 1.0
NE2 A:HIS423 2.0 76.4 1.0
SG A:CYS333 2.1 0.8 1.0
SG A:CYS427 2.1 86.8 1.0
CE1 A:HIS423 2.9 75.0 1.0
CB A:CYS432 2.9 69.2 1.0
CB A:CYS427 3.0 74.8 1.0
CD2 A:HIS423 3.0 72.6 1.0
CB A:CYS333 3.2 78.4 1.0
ND1 A:HIS423 4.0 67.1 1.0
CG A:HIS423 4.1 68.7 1.0
NE2 A:HIS424 4.3 71.5 1.0
CA A:CYS333 4.3 77.3 1.0
CA A:CYS427 4.4 73.3 1.0
CA A:CYS432 4.4 72.2 1.0
C A:CYS333 4.4 79.5 1.0
CB A:ASN429 4.4 66.1 1.0
CD2 A:HIS424 4.7 74.6 1.0
O A:CYS333 4.7 86.6 1.0
N A:VAL334 4.7 71.4 1.0
C A:CYS432 4.8 67.5 1.0
C A:CYS427 5.0 74.1 1.0

Reference:

F.Yuan, Z.Q.Gao, V.Majerciak, L.Bai, M.L.Hu, X.X.Lin, Z.M.Zheng, Y.H.Dong, K.Lan. The Crystal Structure of Kshv ORF57 Reveals Dimeric Active Sites Important For Protein Stability and Function. Plos Pathog. V. 14 07232 2018.
ISSN: ESSN 1553-7374
PubMed: 30096191
DOI: 10.1371/JOURNAL.PPAT.1007232
Page generated: Wed Dec 16 11:25:42 2020

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