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2VOY

CryoEM model of CopA, the copper transporting ATPase from Archaeoglobus fulgidus

Functional Information from GO Data
ChainGOidnamespacecontents
A0046872molecular_functionmetal ion binding
F0005215molecular_functiontransporter activity
F0005524molecular_functionATP binding
F0006812biological_processmonoatomic cation transport
F0016020cellular_componentmembrane
F0016887molecular_functionATP hydrolysis activity
F0019829molecular_functionATPase-coupled monoatomic cation transmembrane transporter activity
I0005215molecular_functiontransporter activity
I0005524molecular_functionATP binding
I0016020cellular_componentmembrane
I0016887molecular_functionATP hydrolysis activity
J0000166molecular_functionnucleotide binding
Functional Information from PROSITE/UniProt
site_idPS00154
Number of Residues7
DetailsATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT
ChainResidueDetails
IASP424-THR430

site_idPS01047
Number of Residues30
DetailsHMA_1 Heavy-metal-associated domain. IeGMtCaACanrIEkrLnkiegvanap.VnF
ChainResidueDetails
AILE9-PHE38

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING:
ChainResidueDetails
IALA627
ILEU631

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10864315, ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1SU4, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T, ECO:0007744|PDB:1VFP, ECO:0007744|PDB:2C9M, ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3BA6, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4NAB, ECO:0007744|PDB:4XOU, ECO:0007744|PDB:5XA7, ECO:0007744|PDB:5XA8
ChainResidueDetails
LTHR799

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10864315, ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1SU4, ECO:0007744|PDB:1T5T, ECO:0007744|PDB:1VFP, ECO:0007744|PDB:2C9M, ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3BA6, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4NAB, ECO:0007744|PDB:4XOU, ECO:0007744|PDB:5XA7, ECO:0007744|PDB:5XA8
ChainResidueDetails
LASP800

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10864315, ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1SU4, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T, ECO:0007744|PDB:1VFP, ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3BA6, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4NAB, ECO:0007744|PDB:4XOU
ChainResidueDetails
HILE307

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10864315, ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1SU4, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T, ECO:0007744|PDB:1VFP, ECO:0007744|PDB:2C9M, ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3BA6, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4XOU, ECO:0007744|PDB:5XA7, ECO:0007744|PDB:5XA8
ChainResidueDetails
HGLU309

Catalytic Information from CSA
site_idMCSA1
Number of Residues
DetailsM-CSA 849
ChainResidueDetails

220113

PDB entries from 2024-05-22

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