Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

8TX6

Crystal structure of an engineered variant of galactose oxidase, GOaseRd7BB, from Fusarium graminearum

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0016491molecular_functionoxidoreductase activity
A0045480molecular_functiongalactose oxidase activity
A0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DGNQNGWIGrhEV
ChainResidueDetails
AASP75-VAL87

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues147
DetailsDomain: {"description":"F5/8 type C","evidences":[{"source":"PROSITE-ProRule","id":"PRU00081","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues45
DetailsRepeat: {"description":"Kelch 1"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues42
DetailsRepeat: {"description":"Kelch 2"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues54
DetailsRepeat: {"description":"Kelch 4"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues52
DetailsRepeat: {"description":"Kelch 5"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsActive 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"}]}}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsCross-link: {"description":"3'-(S-cysteinyl)-tyrosine (Cys-Tyr)"}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 322
ChainResidueDetails
ACYS228activator, covalently attached, metal ligand
ATYR272activator, hydrogen radical acceptor, hydrogen radical donor, metal ligand
APHE290activator, radical stabiliser
ATYR495activator, metal ligand, proton acceptor, proton donor
AHIS496metal ligand
AHIS581metal ligand

238895

PDB entries from 2025-07-16

PDB statisticsPDBj update infoContact PDBjnumon