Function and Biology

SOLUTION STRUCTURE OF THE YEAST COPPER TRANSPORTER DOMAIN CCC2A IN THE APO AND CU(I) LOADED STATES

Source organism: Saccharomyces cerevisiae
Biochemical function: metal ion binding
Biological process: not assigned
Cellular component: not assigned

EC 7.2.2.8: P-type Cu(+) transporter

Reaction catalysed:
ATP + H(2)O + Cu(+)(Side 1) = ADP + phosphate + Cu(+)(Side 2)
Systematic name:
ATP phosphohydrolase (P-type, Cu(+)-exporting)
Alternative Name(s):
  • ATP7A
  • ATP7B
  • CopA
  • Cu(+)-exporting ATPase

GO terms

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Sequence family

Pfam Protein family (Pfam)
PF00403
Domain description: Heavy-metal-associated domain
Occurring in:
  1. Copper-transporting ATPase
The deposited structure of PDB entry 1fvq contains 1 copy of Pfam domain PF00403 (Heavy-metal-associated domain) in Copper-transporting ATPase. Showing 1 copy in chain A.

InterPro InterPro annotations
IPR006121
Domain description: Heavy metal-associated domain, HMA
Occurring in:
  1. Copper-transporting ATPase
IPR017969
Domain description: Heavy-metal-associated, conserved site
Occurring in:
  1. Copper-transporting ATPase
IPR036163
Domain description: Heavy metal-associated domain superfamily
Occurring in:
  1. Copper-transporting ATPase

Structure domain

CATH CATH domain
3.30.70.100
Class: Alpha Beta
Architecture: 2-Layer Sandwich
Topology: Alpha-Beta Plaits
Homology: Alpha-Beta Plaits
Occurring in:
  1. Copper-transporting ATPase
The deposited structure of PDB entry 1fvq contains 1 copy of CATH domain 3.30.70.100 (Alpha-Beta Plaits) in Copper-transporting ATPase. Showing 1 copy in chain A.
SCOP SCOP annotation
55009
Class: Alpha and beta proteins (a+b)
Fold: Ferredoxin-like
Superfamily: HMA, heavy metal-associated domain
Occurring in:
  1. Copper-transporting ATPase
The deposited structure of PDB entry 1fvq contains 1 copy of SCOP domain 55009 (HMA, heavy metal-associated domain) in Copper-transporting ATPase. Showing 1 copy in chain A.