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4BEV

ATPase crystal structure with bound phosphate analogue

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
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 900
ChainResidue
AASP426
ATHR428
AASP624
AMGF950
AHOH2002

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE MGF A 950
ChainResidue
ALEU576
ATHR577
AGLY578
ALYS605
AASN627
AMG900
AHOH2001
ATHR277
AASP426
ALYS427
ATHR428

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 Residues160
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
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 Residues3
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 Residues4
DetailsSite: {"description":"Important for copper transport","evidences":[{"source":"PubMed","id":"24317491","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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