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8TX5

Crystal structure of an engineered variant of galactose oxidase, GOaseRd4BB, from Fusarium graminearum

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0016491molecular_functionoxidoreductase activity
A0045480molecular_functiongalactose oxidase activity
A0046872molecular_functionmetal ion binding
B0005576cellular_componentextracellular region
B0016491molecular_functionoxidoreductase activity
B0045480molecular_functiongalactose oxidase activity
B0046872molecular_functionmetal ion binding
C0005576cellular_componentextracellular region
C0016491molecular_functionoxidoreductase activity
C0045480molecular_functiongalactose oxidase activity
C0046872molecular_functionmetal ion binding
D0005576cellular_componentextracellular region
D0016491molecular_functionoxidoreductase activity
D0045480molecular_functiongalactose oxidase activity
D0046872molecular_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 Residues588
DetailsDomain: {"description":"F5/8 type C","evidences":[{"source":"PROSITE-ProRule","id":"PRU00081","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues180
DetailsRepeat: {"description":"Kelch 1"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues168
DetailsRepeat: {"description":"Kelch 2"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues196
DetailsRepeat: {"description":"Kelch 3"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues216
DetailsRepeat: {"description":"Kelch 4"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues208
DetailsRepeat: {"description":"Kelch 5"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
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_FI8
Number of Residues16
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues8
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

site_idMCSA2
Number of Residues6
DetailsM-CSA 322
ChainResidueDetails
BCYS228activator, covalently attached, metal ligand
BTYR272activator, hydrogen radical acceptor, hydrogen radical donor, metal ligand
BPHE290activator, radical stabiliser
BTYR495activator, metal ligand, proton acceptor, proton donor
BHIS496metal ligand
BHIS581metal ligand

site_idMCSA3
Number of Residues6
DetailsM-CSA 322
ChainResidueDetails
CCYS228activator, covalently attached, metal ligand
CTYR272activator, hydrogen radical acceptor, hydrogen radical donor, metal ligand
CPHE290activator, radical stabiliser
CTYR495activator, metal ligand, proton acceptor, proton donor
CHIS496metal ligand
CHIS581metal ligand

site_idMCSA4
Number of Residues6
DetailsM-CSA 322
ChainResidueDetails
DCYS228activator, covalently attached, metal ligand
DTYR272activator, hydrogen radical acceptor, hydrogen radical donor, metal ligand
DPHE290activator, radical stabiliser
DTYR495activator, metal ligand, proton acceptor, proton donor
DHIS496metal ligand
DHIS581metal ligand

247536

PDB entries from 2026-01-14

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