2EIB
Crystal Structure of Galactose Oxidase, W290H mutant
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CU A 700 |
Chain | Residue |
A | PHE227 |
A | TYR272 |
A | TYR495 |
A | HIS496 |
A | HIS581 |
A | ACT703 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA A 702 |
Chain | Residue |
A | THR37 |
A | ALA141 |
A | GLU142 |
A | LYS29 |
A | ASP32 |
A | ASN34 |
site_id | AC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE SO4 A 704 |
Chain | Residue |
A | ARG122 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ACT A 701 |
Chain | Residue |
A | ARG371 |
A | ALA378 |
A | ALA381 |
A | THR398 |
A | PHE399 |
A | GLY400 |
A | HIS415 |
A | HOH768 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT A 703 |
Chain | Residue |
A | TYR272 |
A | HIS290 |
A | TYR495 |
A | CU700 |
A | HOH975 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT A 705 |
Chain | Residue |
A | GLY195 |
A | GLY196 |
A | HOH1023 |
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 | HIS290 |
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 | HIS290 | activator, radical stabiliser |
A | TYR495 | activator, metal ligand, proton acceptor, proton donor |
A | HIS496 | metal ligand |
A | HIS581 | metal ligand |