4BYG
ATPase crystal structure
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005215 | molecular_function | transporter activity |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006811 | biological_process | monoatomic ion transport |
| A | 0006812 | biological_process | monoatomic cation transport |
| A | 0006825 | biological_process | copper ion transport |
| A | 0006878 | biological_process | intracellular copper ion homeostasis |
| A | 0015662 | molecular_function | P-type ion transporter activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0019829 | molecular_function | ATPase-coupled monoatomic cation transmembrane transporter activity |
| A | 0043682 | molecular_function | P-type divalent copper transporter activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0046915 | molecular_function | transition metal ion transmembrane transporter activity |
| A | 0055070 | biological_process | copper ion homeostasis |
| A | 0060003 | biological_process | copper ion export |
| A | 0140581 | molecular_function | P-type monovalent copper transporter activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ALF A 995 |
| Chain | Residue |
| A | ASP426 |
| A | MG996 |
| A | HOH2014 |
| A | HOH2015 |
| A | HOH2021 |
| A | LYS427 |
| A | THR428 |
| A | THR577 |
| A | GLY578 |
| A | LYS605 |
| A | ASP624 |
| A | ASN627 |
| A | ASP628 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 996 |
| Chain | Residue |
| A | ASP426 |
| A | THR428 |
| A | ASP624 |
| A | ALF995 |
| A | HOH2015 |
| A | HOH2021 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE K A 997 |
| Chain | Residue |
| A | MET100 |
| A | MET711 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 15P A 1000 |
| Chain | Residue |
| A | PHE108 |
| A | SER110 |
| A | ASN112 |
| A | TRP116 |
| A | LEU120 |
| A | LEU168 |
| A | SER676 |
| A | GLN680 |
| A | PHE683 |
| A | TYR688 |
| A | SER723 |
| A | ILE726 |
| A | ASN727 |
| A | ARG730 |
Functional Information from PROSITE/UniProt
| site_id | PS00154 |
| Number of Residues | 7 |
| Details | ATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT |
| Chain | Residue | Details |
| A | ASP426-THR432 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 160 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active 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."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Site: {"description":"Important for copper transport","evidences":[{"source":"PubMed","id":"24317491","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
