Loading
PDBj
English日本語简体中文繁體中文한국어
✖
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help
SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

3RFU

Crystal structure of a copper-transporting PIB-type ATPase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion 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
A0006878biological_processintracellular copper ion homeostasis
A0015662molecular_functionP-type ion transporter activity
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
A0019829molecular_functionATPase-coupled monoatomic cation transmembrane transporter activity
A0043682molecular_functionP-type divalent copper transporter activity
A0046872molecular_functionmetal ion binding
A0046915molecular_functiontransition metal ion transmembrane transporter activity
A0055070biological_processcopper ion homeostasis
A0060003biological_processcopper ion export
A0140581molecular_functionP-type monovalent copper transporter activity
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion 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
B0006878biological_processintracellular copper ion homeostasis
B0015662molecular_functionP-type ion transporter activity
B0016020cellular_componentmembrane
B0016887molecular_functionATP hydrolysis activity
B0019829molecular_functionATPase-coupled monoatomic cation transmembrane transporter activity
B0043682molecular_functionP-type divalent copper transporter activity
B0046872molecular_functionmetal ion binding
B0046915molecular_functiontransition metal ion transmembrane transporter activity
B0055070biological_processcopper ion homeostasis
B0060003biological_processcopper ion export
B0140581molecular_functionP-type monovalent copper transporter activity
C0000166molecular_functionnucleotide binding
C0000287molecular_functionmagnesium ion binding
C0005215molecular_functiontransporter activity
C0005507molecular_functioncopper ion binding
C0005524molecular_functionATP binding
C0005886cellular_componentplasma membrane
C0006811biological_processmonoatomic ion transport
C0006812biological_processmonoatomic cation transport
C0006825biological_processcopper ion transport
C0006878biological_processintracellular copper ion homeostasis
C0015662molecular_functionP-type ion transporter activity
C0016020cellular_componentmembrane
C0016887molecular_functionATP hydrolysis activity
C0019829molecular_functionATPase-coupled monoatomic cation transmembrane transporter activity
C0043682molecular_functionP-type divalent copper transporter activity
C0046872molecular_functionmetal ion binding
C0046915molecular_functiontransition metal ion transmembrane transporter activity
C0055070biological_processcopper ion homeostasis
C0060003biological_processcopper ion export
C0140581molecular_functionP-type monovalent copper transporter activity
D0000166molecular_functionnucleotide binding
D0000287molecular_functionmagnesium ion binding
D0005215molecular_functiontransporter activity
D0005507molecular_functioncopper ion binding
D0005524molecular_functionATP binding
D0005886cellular_componentplasma membrane
D0006811biological_processmonoatomic ion transport
D0006812biological_processmonoatomic cation transport
D0006825biological_processcopper ion transport
D0006878biological_processintracellular copper ion homeostasis
D0015662molecular_functionP-type ion transporter activity
D0016020cellular_componentmembrane
D0016887molecular_functionATP hydrolysis activity
D0019829molecular_functionATPase-coupled monoatomic cation transmembrane transporter activity
D0043682molecular_functionP-type divalent copper transporter activity
D0046872molecular_functionmetal ion binding
D0046915molecular_functiontransition metal ion transmembrane transporter activity
D0055070biological_processcopper ion homeostasis
D0060003biological_processcopper ion export
D0140581molecular_functionP-type monovalent copper transporter activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ALF A 995
ChainResidue
ATHR277
AMG996
AASP426
ALYS427
ATHR428
ATHR577
AGLY578
AASP624
AASN627
AASP628
site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 996
ChainResidue
ATHR428
AASP624
AALF995
site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE K A 997
ChainResidue
AGLU99
AGLU189
site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ALF B 995
ChainResidue
BTHR277
BASP426
BLYS427
BTHR428
BTHR577
BGLY578
BASN627
BASP628
BMG996
site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 996
ChainResidue
BASP426
BTHR428
BASP624
BALF995
site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE K B 997
ChainResidue
BGLU99
site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ALF C 995
ChainResidue
CTHR277
CASP426
CLYS427
CTHR428
CTHR577
CGLY578
CASN627
CASP628
CMG996
site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG C 996
ChainResidue
CASP426
CTHR428
CASP624
CALF995
site_idAC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE K C 997
ChainResidue
CGLU99
site_idBC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ALF D 995
ChainResidue
DTHR277
DASP426
DLYS427
DTHR428
DTHR577
DGLY578
DASN627
DASP628
DMG996
site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG D 996
ChainResidue
DASP426
DTHR428
DASP624
DALF995
site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE K D 997
ChainResidue
DGLU99
Functional Information from PROSITE/UniProt
site_idPS00154
Number of Residues7
DetailsATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT
ChainResidueDetails
AASP426-THR432
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues640
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"4-aspartylphosphate intermediate","evidences":[{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"MAR-2013","submissionDatabase":"PDB data bank","title":"ATPase crystal structure with bound phosphate analogue.","authors":["Mattle D.","Drachmann N.D.","Liu X.Y.","Gourdon P.","Pedersen B.P.","Morth P.","Wang J.","Nissen P."]}},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"JUL-2013","submissionDatabase":"PDB data bank","title":"Dephosphorylation of PIB-type Cu(I)-ATPases as studied by metallofluoride complexes.","authors":["Mattle D.","Drachmann N.D.","Liu X.Y.","Pedersen B.P.","Morth J.P.","Wang J.","Gourdon P.","Nissen P."]}}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24317491","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2013","submissionDatabase":"PDB data bank","title":"ATPase crystal structure with bound phosphate analogue.","authors":["Mattle D.","Drachmann N.D.","Liu X.Y.","Gourdon P.","Pedersen B.P.","Morth P.","Wang J.","Nissen P."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2013","submissionDatabase":"PDB data bank","title":"Dephosphorylation of PIB-type Cu(I)-ATPases as studied by metallofluoride complexes.","authors":["Mattle D.","Drachmann N.D.","Liu X.Y.","Pedersen B.P.","Morth J.P.","Wang J.","Gourdon P.","Nissen P."]}},{"source":"PDB","id":"4BBJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BEV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BYG","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues16
DetailsSite: {"description":"Important for copper transport","evidences":[{"source":"PubMed","id":"24317491","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon