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Zinc in PDB 2kqb: First Pbz Domain of Human Aplf Protein

Enzymatic activity of First Pbz Domain of Human Aplf Protein

All present enzymatic activity of First Pbz Domain of Human Aplf Protein:
4.2.99.18;

Zinc Binding Sites:

The binding sites of Zinc atom in the First Pbz Domain of Human Aplf Protein (pdb code 2kqb). 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 First Pbz Domain of Human Aplf Protein, PDB code: 2kqb:

Zinc binding site 1 out of 1 in 2kqb

Go back to Zinc Binding Sites List in 2kqb
Zinc binding site 1 out of 1 in the First Pbz Domain of Human Aplf Protein


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of First Pbz Domain of Human Aplf Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1001

b:0.0
occ:1.00
NE2 A:HIS392 2.0 0.0 1.0
NE2 A:HIS398 2.0 0.0 1.0
SG A:CYS379 2.3 0.0 1.0
SG A:CYS385 2.5 0.0 1.0
CE1 A:HIS392 3.0 0.0 1.0
CE1 A:HIS398 3.1 0.0 1.0
CD2 A:HIS398 3.1 0.0 1.0
CD2 A:HIS392 3.1 0.0 1.0
HB2 A:CYS379 3.1 0.0 1.0
HE1 A:HIS392 3.2 0.0 1.0
CB A:CYS379 3.3 0.0 1.0
HD2 A:HIS398 3.3 0.0 1.0
HE1 A:HIS398 3.3 0.0 1.0
HD2 A:HIS392 3.4 0.0 1.0
HB2 A:CYS385 3.4 0.0 1.0
CB A:CYS385 3.6 0.0 1.0
HB2 A:PHE396 3.6 0.0 1.0
HB3 A:CYS379 3.6 0.0 1.0
HB3 A:CYS385 4.1 0.0 1.0
HB3 A:PHE396 4.1 0.0 1.0
ND1 A:HIS392 4.2 0.0 1.0
ND1 A:HIS398 4.2 0.0 1.0
CG A:HIS398 4.2 0.0 1.0
CG A:HIS392 4.2 0.0 1.0
CB A:PHE396 4.3 0.0 1.0
HG3 A:ARG387 4.4 0.0 1.0
HE A:ARG387 4.4 0.0 1.0
CA A:CYS379 4.6 0.0 1.0
HA A:CYS379 4.7 0.0 1.0
HB2 A:TYR381 4.7 0.0 1.0
HG2 A:ARG387 4.8 0.0 1.0
HA A:CYS385 4.8 0.0 1.0
CA A:CYS385 4.8 0.0 1.0
HD2 A:TYR381 5.0 0.0 1.0
O A:ARG387 5.0 0.0 1.0
H A:TYR381 5.0 0.0 1.0

Reference:

S.Eustermann, C.Brockmann, P.V.Mehrotra, J.C.Yang, D.Loakes, S.C.West, I.Ahel, D.Neuhaus. Solution Structures of the Two Pbz Domains From Human Aplf and Their Interaction with Poly(Adp-Ribose). Nat.Struct.Mol.Biol. V. 17 241 2010.
ISSN: ISSN 1545-9993
PubMed: 20098424
DOI: 10.1038/NSMB.1747
Page generated: Thu Oct 17 01:38:37 2024

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