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Zinc in PDB 1m9o: uc(Nmr) Structure of the First Zinc Binding Domain of NUP475/Ttp/TIS11

Zinc Binding Sites:

The binding sites of Zinc atom in the uc(Nmr) Structure of the First Zinc Binding Domain of NUP475/Ttp/TIS11 (pdb code 1m9o). 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 First Zinc Binding Domain of NUP475/Ttp/TIS11, PDB code: 1m9o:

Zinc binding site 1 out of 1 in 1m9o

Go back to Zinc Binding Sites List in 1m9o
Zinc binding site 1 out of 1 in the uc(Nmr) Structure of the First Zinc Binding Domain of NUP475/Ttp/TIS11


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 First Zinc Binding Domain of NUP475/Ttp/TIS11 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn78

b:0.0
occ:1.00
NE2 A:HIS34 2.0 0.0 1.0
SG A:CYS30 2.3 0.0 1.0
SG A:CYS24 2.3 0.0 1.0
SG A:CYS15 2.3 0.0 1.0
CD2 A:HIS34 3.0 0.0 1.0
CE1 A:HIS34 3.0 0.0 1.0
HD2 A:HIS34 3.2 0.0 1.0
HA A:CYS24 3.2 0.0 1.0
HE1 A:HIS34 3.2 0.0 1.0
HB2 A:CYS15 3.2 0.0 1.0
HB3 A:TYR18 3.3 0.0 1.0
CB A:CYS30 3.4 0.0 1.0
HB2 A:CYS30 3.4 0.0 1.0
CB A:CYS24 3.5 0.0 1.0
HB3 A:CYS30 3.5 0.0 1.0
CB A:CYS15 3.5 0.0 1.0
HB3 A:CYS24 3.6 0.0 1.0
CA A:CYS24 3.8 0.0 1.0
HA A:SER19 3.9 0.0 1.0
HB2 A:TYR18 4.0 0.0 1.0
CG A:HIS34 4.1 0.0 1.0
ND1 A:HIS34 4.1 0.0 1.0
CB A:TYR18 4.2 0.0 1.0
HD2 A:TYR18 4.2 0.0 1.0
HB3 A:CYS15 4.2 0.0 1.0
HA A:CYS15 4.2 0.0 1.0
HB2 A:CYS24 4.4 0.0 1.0
N A:SER19 4.5 0.0 1.0
CA A:CYS15 4.5 0.0 1.0
HA2 A:GLY27 4.6 0.0 1.0
H A:SER19 4.6 0.0 1.0
C A:TYR18 4.6 0.0 1.0
CA A:SER19 4.7 0.0 1.0
H A:TYR26 4.7 0.0 1.0
CA A:CYS30 4.8 0.0 1.0
C A:CYS24 4.8 0.0 1.0
H A:CYS30 4.9 0.0 1.0
H A:ALA28 4.9 0.0 1.0
N A:CYS24 4.9 0.0 1.0
O A:TYR18 4.9 0.0 1.0
HD1 A:HIS34 5.0 0.0 1.0

Reference:

B.T.Amann, M.T.Worthington, J.M.Berg. A CYS3HIS Zinc-Binding Domain From NUP475/Tristetraproline: A Novel Fold with A Disklike Structure Biochemistry V. 42 217 2003.
ISSN: ISSN 0006-2960
PubMed: 12515557
DOI: 10.1021/BI026988M
Page generated: Sun Oct 13 05:29:18 2024

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