› 3dxs

X-ray diffraction
1.7Å resolution

Crystal structure of a copper binding domain from HMA7, a P-type ATPase

Released:
DOI: 10.2210/pdb3dxs/pdb
PDB entry 3dxs coloured by chain, front view.
PDB entry 3dxs coloured by chain, side view.
PDB entry 3dxs coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Metal binding affinities of Arabidopsis zinc and copper transporters: selectivities match the relative, but not the absolute, affinities of their amino-terminal domains.
Zimmermann M, Clarke O, Gulbis JM, Keizer DW, Jarvis RS, Cobbett CS, Hinds MG, Xiao Z, Wedd AG
Biochemistry 48 11640-54 (2009)
PMID: 19883117

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O + Cu(+)(Side 1) = ADP + phosphate + Cu(+)(Side 2)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193421 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Copper-transporting ATPase RAN1 Chain: X
Molecule details ›
Chain: X
Length: 74 amino acids
Theoretical weight: 8.07 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9S7J8 (Residues: 55-128; Coverage: 7%)
Gene names: At5g44790, HMA7, K23L20.14, RAN1, T19K24.18
Sequence domains: Heavy-metal-associated domain
Structure domains: Alpha-Beta Plaits

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand LI 1 x LI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 27.374Å b: 44.529Å c: 49.223Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.142 0.142 0.16
Expression system: Escherichia coli

Quick links

Citations

6 review citations

The challenges of determining metal-protein affinities.
Xiao et al. (2010)
5 more

2 mentions without citation

Specific recognition of two MAX effectors by integrated HMA domains in plant immune receptors involves distinct binding surfaces.
Guo et al. (2018)
1 more