2EIC
Crystal Structure of Galactose Oxidase mutant W290F
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 640 |
| Chain | Residue |
| A | LYS29 |
| A | ASP32 |
| A | ASN34 |
| A | THR37 |
| A | ALA141 |
| A | GLU142 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CU1 A 641 |
| Chain | Residue |
| A | TYR495 |
| A | HIS496 |
| A | HIS581 |
| A | PHE227 |
| A | CYS228 |
| A | TYR272 |
Functional Information from PROSITE/UniProt
| site_id | PS00018 |
| Number of Residues | 13 |
| Details | EF_HAND_1 EF-hand calcium-binding domain. DGNQNGWIGrhEV |
| Chain | Residue | Details |
| A | ASP75-VAL87 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 147 |
| Details | Domain: {"description":"F5/8 type C","evidences":[{"source":"PROSITE-ProRule","id":"PRU00081","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 45 |
| Details | Repeat: {"description":"Kelch 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 42 |
| Details | Repeat: {"description":"Kelch 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 49 |
| Details | Repeat: {"description":"Kelch 3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 54 |
| Details | Repeat: {"description":"Kelch 4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 52 |
| Details | Repeat: {"description":"Kelch 5"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1997","firstPage":"327","lastPage":"335","volume":"2","journal":"J. Biol. Inorg. Chem.","title":"Structure and mechanism of galactose oxidase: catalytic role of tyrosine 495.","authors":["Reynolds M.P.","Baron A.J.","Wilmot C.M.","Vinecombe E.","Stevens C.","Phillips S.E.V.","Knowles P.F.","McPherson M.J."],"citationCrossReferences":[{"database":"DOI","id":"10.1007/s007750050139"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"3'-(S-cysteinyl)-tyrosine (Cys-Tyr)"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1gog |
| Chain | Residue | Details |
| A | TYR272 | |
| A | CYS228 | |
| A | TYR495 | |
| A | PHE290 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 322 |
| Chain | Residue | Details |
| A | CYS228 | activator, covalently attached, metal ligand |
| A | TYR272 | activator, hydrogen radical acceptor, hydrogen radical donor, metal ligand |
| A | PHE290 | activator, radical stabiliser |
| A | TYR495 | activator, metal ligand, proton acceptor, proton donor |
| A | HIS496 | metal ligand |
| A | HIS581 | metal ligand |
