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Zinc in PDB 5kvp: Solution Structure of the Catalytic Domain of Zoocin A

Zinc Binding Sites:

The binding sites of Zinc atom in the Solution Structure of the Catalytic Domain of Zoocin A (pdb code 5kvp). 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 Solution Structure of the Catalytic Domain of Zoocin A, PDB code: 5kvp:

Zinc binding site 1 out of 1 in 5kvp

Go back to Zinc Binding Sites List in 5kvp
Zinc binding site 1 out of 1 in the Solution Structure of the Catalytic Domain of Zoocin A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Solution Structure of the Catalytic Domain of Zoocin A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn201

b:0.0
occ:1.00
OD1 A:ASP38 2.0 0.0 1.0
NE2 A:HIS34 2.0 0.0 1.0
O A:UNL202 2.0 0.0 1.0
ND1 A:HIS122 2.1 0.0 1.0
OD2 A:ASP38 2.5 0.0 1.0
CG A:ASP38 2.5 0.0 1.0
HB2 A:HIS122 2.8 0.0 1.0
CE1 A:HIS34 3.0 0.0 1.0
CE1 A:HIS122 3.1 0.0 1.0
CG A:HIS122 3.1 0.0 1.0
CD2 A:HIS34 3.1 0.0 1.0
HE1 A:HIS34 3.2 0.0 1.0
HE1 A:HIS122 3.3 0.0 1.0
HD2 A:HIS34 3.4 0.0 1.0
CB A:HIS122 3.4 0.0 1.0
HA A:HIS122 3.7 0.0 1.0
HE2 A:HIS120 3.9 0.0 1.0
CB A:ASP38 4.0 0.0 1.0
O A:VAL37 4.1 0.0 1.0
HE1 A:HIS89 4.1 0.0 1.0
ND1 A:HIS34 4.2 0.0 1.0
CA A:HIS122 4.2 0.0 1.0
NE2 A:HIS122 4.2 0.0 1.0
CD2 A:HIS122 4.2 0.0 1.0
CG A:HIS34 4.2 0.0 1.0
HD1 A:HIS89 4.3 0.0 1.0
HB3 A:HIS122 4.3 0.0 1.0
HD2 A:HIS120 4.4 0.0 1.0
C A:VAL37 4.4 0.0 1.0
HA A:ASP38 4.4 0.0 1.0
CE1 A:HIS89 4.4 0.0 1.0
ND1 A:HIS89 4.5 0.0 1.0
HB2 A:ASP38 4.5 0.0 1.0
HB3 A:ASP38 4.6 0.0 1.0
CA A:ASP38 4.6 0.0 1.0
N A:ASP38 4.7 0.0 1.0
NE2 A:HIS120 4.7 0.0 1.0
H A:VAL37 4.9 0.0 1.0
N A:VAL37 4.9 0.0 1.0
HA3 A:GLY36 4.9 0.0 1.0
CD2 A:HIS120 4.9 0.0 1.0
HB1 A:ALA88 4.9 0.0 1.0
H A:PHE123 4.9 0.0 1.0

Reference:

M.Xing, R.S.Simmonds, R.Timkovich. Solution Structure of the CYS74 to ALA74 Mutant of the Recombinant Catalytic Domain of Zoocin A. Proteins V. 85 177 2017.
ISSN: ESSN 1097-0134
PubMed: 27699884
DOI: 10.1002/PROT.25178
Page generated: Thu Aug 21 04:27:01 2025

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