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Zinc in PDB 1mwz: Solution Structure of the N-Terminal Domain of Znta in the Zn(II)-Form

Enzymatic activity of Solution Structure of the N-Terminal Domain of Znta in the Zn(II)-Form

All present enzymatic activity of Solution Structure of the N-Terminal Domain of Znta in the Zn(II)-Form:
3.6.3.3; 3.6.3.5;

Zinc Binding Sites:

The binding sites of Zinc atom in the Solution Structure of the N-Terminal Domain of Znta in the Zn(II)-Form (pdb code 1mwz). 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 N-Terminal Domain of Znta in the Zn(II)-Form, PDB code: 1mwz:

Zinc binding site 1 out of 1 in 1mwz

Go back to Zinc Binding Sites List in 1mwz
Zinc binding site 1 out of 1 in the Solution Structure of the N-Terminal Domain of Znta in the Zn(II)-Form


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 N-Terminal Domain of Znta in the Zn(II)-Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn75

b:0.8
occ:1.00
OD1 A:ASP14 2.1 1.4 1.0
SG A:CYS15 2.4 0.7 1.0
SG A:CYS18 2.4 0.6 1.0
CG A:ASP14 2.7 0.8 1.0
OD2 A:ASP14 2.8 1.3 1.0
H A:ASP14 3.0 0.5 1.0
HB2 A:CYS15 3.4 0.4 1.0
CB A:CYS15 3.6 0.5 1.0
CB A:CYS18 3.6 0.4 1.0
HB2 A:CYS18 3.7 0.4 1.0
H A:CYS15 3.7 0.6 1.0
N A:CYS15 3.9 0.5 1.0
N A:ASP14 3.9 0.4 1.0
HB3 A:CYS18 3.9 0.5 1.0
CB A:ASP14 4.0 0.8 1.0
C A:ASP14 4.3 0.5 1.0
CA A:ASP14 4.3 0.5 1.0
HA A:MET13 4.3 0.4 1.0
O A:GLY12 4.3 1.4 1.0
CA A:CYS15 4.4 0.4 1.0
HB3 A:CYS15 4.4 0.5 1.0
HB3 A:ASP14 4.6 0.8 1.0
HB2 A:ASP14 4.6 0.9 1.0
HH A:TYR65 4.7 1.5 1.0
H A:CYS18 4.7 0.3 1.0
HE1 A:TYR65 4.9 3.2 1.0
CA A:CYS18 5.0 0.3 1.0
C A:MET13 5.0 0.4 1.0

Reference:

L.Banci, I.Bertini, S.Ciofi-Baffoni, L.A.Finney, C.E.Outten, T.V.O'halloran. A New Zinc-Protein Coordination Site in Intracellular Metal Trafficking: Solution Structure of the Apo and Zn(II) Forms of Znta (46-118) J.Mol.Biol. V. 323 883 2002.
ISSN: ISSN 0022-2836
PubMed: 12417201
DOI: 10.1016/S0022-2836(02)01007-0
Page generated: Wed Oct 16 17:03:46 2024

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