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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
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
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
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
ALEU102-PRO122
BLEU129-SER149
BVAL160-VAL180
BPHE187-LEU204
BALA340-ILE360
BLEU365-GLY385
BILE681-VAL701
BGLU705-LEU725
ALEU129-SER149
AVAL160-VAL180
APHE187-LEU204
AALA340-ILE360
ALEU365-GLY385
AILE681-VAL701
AGLU705-LEU725
BLEU102-PRO122

site_idSWS_FT_FI2
Number of Residues30
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
ATYR123-GLN128
ALEU181-SER186
AALA361-PRO364
APHE702-PRO704
BTYR123-GLN128
BLEU181-SER186
BALA361-PRO364
BPHE702-PRO704

site_idSWS_FT_FI3
Number of Residues874
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
AALA150-ASP159
AGLU205-VAL339
ALEU386-LEU680
BALA150-ASP159
BGLU205-VAL339
BLEU386-LEU680

site_idSWS_FT_FI4
Number of Residues2
DetailsACT_SITE: 4-aspartylphosphate intermediate => ECO:0000250
ChainResidueDetails
AASP424
BASP424

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00280
ChainResidueDetails
ACYS27
ACYS30
BCYS27
BCYS30

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AGLU457
AGLY490
BGLU457
BGLY490

site_idSWS_FT_FI7
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AASP618
AASP622
BASP618
BASP622

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PDB entries from 2024-10-30

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