Zinc in PDB 3dxs: Crystal Structure of A Copper Binding Domain From HMA7, A P- Type Atpase

All present enzymatic activity of Crystal Structure of A Copper Binding Domain From HMA7, A P- Type Atpase:
3.6.3.4;

The structure of Crystal Structure of A Copper Binding Domain From HMA7, A P- Type Atpase, PDB code: 3dxs was solved by M.Zimmermann, Z.Xiao, O.B.Clarke, J.M.Gulbis, A.G.Wedd, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	27.374, 44.529, 49.223, 90.00, 90.00, 90.00
R / Rfree (%)	14.2 / 16

The binding sites of Zinc atom in the Crystal Structure of A Copper Binding Domain From HMA7, A P- Type Atpase (pdb code 3dxs). 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 Crystal Structure of A Copper Binding Domain From HMA7, A P- Type Atpase, PDB code: 3dxs:

Zinc binding site 1 out of 1 in the Crystal Structure of A Copper Binding Domain From HMA7, A P- Type Atpase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of A Copper Binding Domain From HMA7, A P- Type Atpase within 5.0Å range: probe atom residue distance (Å) B Occ X:Zn75 b:5.8 occ:0.75 SG X:CYS16 2.2 10.1 1.0 SG X:CYS13 2.2 10.4 1.0 CB X:CYS13 3.4 9.4 1.0 CB X:CYS16 3.4 8.6 1.0 N X:CYS13 3.5 9.1 1.0 N X:CYS16 3.7 9.1 1.0 CA X:CYS13 3.9 9.3 1.0 CA X:CYS16 3.9 8.9 1.0 OG1 X:THR12 4.1 9.3 1.0 C X:THR12 4.2 9.2 1.0 O X:CYS13 4.3 9.2 1.0 N X:THR12 4.3 9.6 1.0 C X:CYS13 4.3 9.2 1.0 CA X:THR12 4.7 9.5 1.0 C X:ALA15 4.7 9.4 1.0 CB X:ALA15 4.8 9.9 1.0 O X:THR12 4.9 9.3 1.0 N X:ALA15 5.0 9.7 1.0

M.Zimmermann, O.B.Clarke, J.M.Gulbis, D.W.Keizer, R.S.Jarvis, C.S.Cobbett, M.G.Hinds, Z.Xiao, A.G.Wedd. Metal Binding Affinities of Arabidopsis Zinc and Copper Transporters: Selectivities Match the Relative, But Not the Absolute, Affinities of Their Amino-Terminal Domains. Biochemistry V. 48 11640 2009.
ISSN: ISSN 0006-2960
PubMed: 19883117
DOI: 10.1021/BI901573B