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2EIE

Crystal Structure of Galactose Oxidase complexed with Azide

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0016491molecular_functionoxidoreductase activity
A0045480molecular_functiongalactose oxidase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE AZI A 2391
ChainResidue
APHE194
AHOH1225
APHE227
ATYR272
ATRP290
APHE464
ATYR495
AHIS496
AASN597
ACU700

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CU A 700
ChainResidue
APHE227
ACYS228
ATYR272
ATYR495
AHIS496
AHIS581
AAZI2391

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 Residues49
DetailsRepeat: {"description":"Kelch 3"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues54
DetailsRepeat: {"description":"Kelch 4"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues52
DetailsRepeat: {"description":"Kelch 5"}
ChainResidueDetails

site_idSWS_FT_FI7
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_FI8
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsCross-link: {"description":"3'-(S-cysteinyl)-tyrosine (Cys-Tyr)"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1gog
ChainResidueDetails
ATYR272
ACYS228
ATYR495
ATRP290

site_idMCSA1
Number of Residues6
DetailsM-CSA 322
ChainResidueDetails
ACYS228activator, covalently attached, metal ligand
ATYR272activator, hydrogen radical acceptor, hydrogen radical donor, metal ligand
ATRP290activator, radical stabiliser
ATYR495activator, metal ligand, proton acceptor, proton donor
AHIS496metal ligand
AHIS581metal ligand

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PDB entries from 2026-02-18

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