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

1K3I

Crystal Structure of the Precursor of Galactose Oxidase

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 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

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1gog
ChainResidueDetails
ATYR272
ATYR495
ATRP290

site_idMCSA1
Number of Residues6
DetailsM-CSA 322
ChainResidueDetails
APRO229activator, covalently attached, metal ligand
AALA276activator, hydrogen radical acceptor, hydrogen radical donor, metal ligand
AVAL294activator, radical stabiliser
ASER499activator, metal ligand, proton acceptor, proton donor
ALEU500metal ligand
ATHR585metal ligand

247536

PDB entries from 2026-01-14

PDB statisticsPDBj update infoContact PDBjnumon