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3J09

High resolution helical reconstruction of the bacterial p-type ATPase copper transporter CopA

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005215molecular_functiontransporter activity
A0005507molecular_functioncopper ion binding
A0005524molecular_functionATP binding
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006812biological_processmonoatomic cation transport
A0006825biological_processcopper ion transport
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
A0019829molecular_functionATPase-coupled monoatomic cation transmembrane transporter activity
A0035434biological_processcopper ion transmembrane transport
A0042802molecular_functionidentical protein binding
A0043682molecular_functionP-type divalent copper transporter activity
A0046872molecular_functionmetal ion binding
A0055070biological_processcopper ion homeostasis
A0098655biological_processmonoatomic cation transmembrane transport
A0140581molecular_functionP-type monovalent copper transporter activity
B0000166molecular_functionnucleotide binding
B0005215molecular_functiontransporter activity
B0005507molecular_functioncopper ion binding
B0005524molecular_functionATP binding
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0006812biological_processmonoatomic cation transport
B0006825biological_processcopper ion transport
B0016020cellular_componentmembrane
B0016887molecular_functionATP hydrolysis activity
B0019829molecular_functionATPase-coupled monoatomic cation transmembrane transporter activity
B0035434biological_processcopper ion transmembrane transport
B0042802molecular_functionidentical protein binding
B0043682molecular_functionP-type divalent copper transporter activity
B0046872molecular_functionmetal ion binding
B0055070biological_processcopper ion homeostasis
B0098655biological_processmonoatomic cation transmembrane transport
B0140581molecular_functionP-type monovalent copper transporter activity
Functional Information from PROSITE/UniProt
site_idPS00154
Number of Residues7
DetailsATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT
ChainResidueDetails
AASP424-THR430

site_idPS01199
Number of Residues19
DetailsRIBOSOMAL_L1 Ribosomal protein L1 signature. GvgAaf.LAsvLSTAGvLPR
ChainResidueDetails
AGLY165-ARG183

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues314
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues30
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues874
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues132
DetailsDomain: {"description":"HMA 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00280","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsActive site: {"description":"4-aspartylphosphate intermediate","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00280","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues32
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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