Zinc in PDB 2kqd: First Pbz Domain of Human Aplf Protein in Complex with Ribofuranosyladenosine

All present enzymatic activity of First Pbz Domain of Human Aplf Protein in Complex with Ribofuranosyladenosine:
4.2.99.18;

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

Zinc binding site 1 out of 1 in the First Pbz Domain of Human Aplf Protein in Complex with Ribofuranosyladenosine


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 in Complex with Ribofuranosyladenosine within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1001 b:0.0 occ:1.00 NE2 A:HIS392 1.9 0.0 1.0 NE2 A:HIS398 2.1 0.0 1.0 SG A:CYS379 2.3 0.0 1.0 SG A:CYS385 2.3 0.0 1.0 CE1 A:HIS392 2.9 0.0 1.0 CD2 A:HIS392 3.0 0.0 1.0 HB2 A:CYS379 3.0 0.0 1.0 CD2 A:HIS398 3.1 0.0 1.0 CE1 A:HIS398 3.1 0.0 1.0 CB A:CYS379 3.2 0.0 1.0 HE1 A:HIS392 3.2 0.0 1.0 HD2 A:HIS392 3.3 0.0 1.0 HD2 A:HIS398 3.3 0.0 1.0 HB2 A:CYS385 3.4 0.0 1.0 HE1 A:HIS398 3.4 0.0 1.0 CB A:CYS385 3.5 0.0 1.0 HB3 A:CYS379 3.5 0.0 1.0 HB2 A:PHE396 3.6 0.0 1.0 HB3 A:CYS385 3.9 0.0 1.0 HB3 A:PHE396 4.0 0.0 1.0 ND1 A:HIS392 4.1 0.0 1.0 CG A:HIS392 4.1 0.0 1.0 HA2 A:GLY382 4.3 0.0 1.0 ND1 A:HIS398 4.3 0.0 1.0 CB A:PHE396 4.3 0.0 1.0 CG A:HIS398 4.3 0.0 1.0 HG3 A:ARG387 4.5 0.0 1.0 CA A:CYS379 4.5 0.0 1.0 HG2 A:ARG387 4.6 0.0 1.0 HA A:CYS379 4.7 0.0 1.0 HA A:CYS385 4.7 0.0 1.0 CA A:CYS385 4.8 0.0 1.0 HD3 A:ARG387 4.8 0.0 1.0 H A:TYR381 4.8 0.0 1.0 CG A:PHE396 5.0 0.0 1.0 HD1 A:HIS392 5.0 0.0 1.0

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