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Zinc in PDB 2nbq: uc(Nmr) Structure of the C-Terminal Domain of Human APOBEC3B

Zinc Binding Sites:

The binding sites of Zinc atom in the uc(Nmr) Structure of the C-Terminal Domain of Human APOBEC3B (pdb code 2nbq). 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 uc(Nmr) Structure of the C-Terminal Domain of Human APOBEC3B, PDB code: 2nbq:

Zinc binding site 1 out of 1 in 2nbq

Go back to Zinc Binding Sites List in 2nbq
Zinc binding site 1 out of 1 in the uc(Nmr) Structure of the C-Terminal Domain of Human APOBEC3B


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of uc(Nmr) Structure of the C-Terminal Domain of Human APOBEC3B within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn500

b:0.0
occ:1.00
SG A:CYS289 2.3 0.0 1.0
SG A:CYS284 2.3 0.0 1.0
ND1 A:HIS253 2.3 0.0 1.0
CE1 A:HIS253 3.0 0.0 1.0
CG A:HIS253 3.0 0.0 1.0
HB2 A:CYS289 3.1 0.0 1.0
HB2 A:CYS284 3.2 0.0 1.0
HB3 A:HIS253 3.2 0.0 1.0
HE1 A:HIS253 3.3 0.0 1.0
CB A:CYS289 3.3 0.0 1.0
CB A:CYS284 3.3 0.0 1.0
CB A:HIS253 3.5 0.0 1.0
OE2 A:GLU255 3.7 0.0 1.0
HB2 A:HIS253 3.8 0.0 1.0
HB3 A:CYS284 3.8 0.0 1.0
NE2 A:HIS253 3.9 0.0 1.0
CD2 A:HIS253 3.9 0.0 1.0
H A:CYS289 4.0 0.0 1.0
H A:CYS284 4.0 0.0 1.0
N A:CYS289 4.1 0.0 1.0
HB3 A:CYS289 4.1 0.0 1.0
H A:PHE285 4.2 0.0 1.0
CA A:CYS289 4.2 0.0 1.0
HA A:CYS289 4.4 0.0 1.0
HA3 A:GLY288 4.6 0.0 1.0
CA A:CYS284 4.6 0.0 1.0
HH21 A:ARG211 4.6 0.0 1.0
CD A:GLU255 4.6 0.0 1.0
C A:GLY288 4.7 0.0 1.0
N A:CYS284 4.7 0.0 1.0
HE2 A:HIS253 4.7 0.0 1.0
HB2 A:GLU255 4.7 0.0 1.0
HD2 A:HIS253 4.8 0.0 1.0
HD12 A:LEU256 4.9 0.0 1.0
N A:PHE285 5.0 0.0 1.0
CA A:HIS253 5.0 0.0 1.0
OE1 A:GLU255 5.0 0.0 1.0

Reference:

I.J.Byeon, C.H.Byeon, T.Wu, M.Mitra, D.Singer, J.G.Levin, A.M.Gronenborn. Nuclear Magnetic Resonance Structure of the APOBEC3B Catalytic Domain: Structural Basis For Substrate Binding and Dna Deaminase Activity. Biochemistry V. 55 2944 2016.
ISSN: ISSN 0006-2960
PubMed: 27163633
DOI: 10.1021/ACS.BIOCHEM.6B00382
Page generated: Wed Dec 16 03:43:28 2020

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