1OA1
REDUCED HYBRID CLUSTER PROTEIN (HCP) FROM DESULFOVIBRIO VULGARIS HILDENBOROUGH STRUCTURE AT 1.55A RESOLUTION USING SYNCHROTRON RADIATION.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016661 | molecular_function | oxidoreductase activity, acting on other nitrogenous compounds as donors |
| A | 0042542 | biological_process | response to hydrogen peroxide |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050418 | molecular_function | hydroxylamine reductase activity |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| A | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 A 1554 |
| Chain | Residue |
| A | CYS3 |
| A | LYS23 |
| A | THR71 |
| A | PHE4 |
| A | GLN5 |
| A | CYS6 |
| A | THR9 |
| A | CYS15 |
| A | GLY19 |
| A | MET20 |
| A | CYS21 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF3 A 1555 |
| Chain | Residue |
| A | HIS244 |
| A | GLU268 |
| A | TRP292 |
| A | CYS312 |
| A | CYS406 |
| A | CYS434 |
| A | CYS459 |
| A | GLU494 |
| A | HOH2767 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 1556 |
| Chain | Residue |
| A | ASN273 |
| A | LYS279 |
| A | TYR281 |
| A | PHE284 |
| A | VAL285 |
| A | HOH2817 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 1557 |
| Chain | Residue |
| A | GLY14 |
| A | CYS15 |
| A | THR16 |
| A | VAL17 |
| A | LYS18 |
| A | HOH2818 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11106482","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11941509","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12764602","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18560155","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2000","submissionDatabase":"PDB data bank","title":"Ferricyanide soaked hybrid cluster protein at 1.2A and xenon mapping of the hydrophobic cavity at 1.8A.","authors":["Cooper S.J.","Garner C.D.","Hagen W.R.","Lindley P.F.","Bailey S."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1998","firstPage":"81","lastPage":"95","volume":"3","journal":"J. Biol. Inorg. Chem.","title":"The 'prismane' protein resolved: X-ray structure at 1.7-A and multiple spectroscopy of two novel 4Fe clusters.","authors":["Arendsen A.F.","Hadden J.","Card G.","McAlpine A.S.","Bailey S.","Zaitsev V.","Duke E.H.M.","Lindley P.F.","Kroeckel M.","Trautwein A.X.","Feiters M.C.","Charnock J.M.","Garner C.D.","Marritt S.J.","Thomson A.J.","Kooter I.M.","Johnson M.K.","van den Berg W.A.M.","van Dongen W.M.A.M.","Hagen W.R."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11106482","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11941509","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12764602","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18560155","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2000","submissionDatabase":"PDB data bank","title":"Ferricyanide soaked hybrid cluster protein at 1.2A and xenon mapping of the hydrophobic cavity at 1.8A.","authors":["Cooper S.J.","Garner C.D.","Hagen W.R.","Lindley P.F.","Bailey S."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"via persulfide group","evidences":[{"source":"PubMed","id":"11106482","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11941509","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12764602","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18560155","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2000","submissionDatabase":"PDB data bank","title":"Ferricyanide soaked hybrid cluster protein at 1.2A and xenon mapping of the hydrophobic cavity at 1.8A.","authors":["Cooper S.J.","Garner C.D.","Hagen W.R.","Lindley P.F.","Bailey S."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Cysteine persulfide","evidences":[{"source":"PubMed","id":"11941509","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
