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1KDG

Crystal structure of the flavin domain of cellobiose dehydrogenase

Functional Information from GO Data
ChainGOidnamespacecontents
A0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
A0050660molecular_functionflavin adenine dinucleotide binding
B0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
B0050660molecular_functionflavin adenine dinucleotide binding
Functional Information from PROSITE/UniProt
site_idPS00623
Number of Residues24
DetailsGMC_OXRED_1 GMC oxidoreductases signature 1. GClVGGGTsVNgalYwyPndgdfS
ChainResidueDetails
AGLY299-SER322

site_idPS00624
Number of Residues15
DetailsGMC_OXRED_2 GMC oxidoreductases signature 2. GAfgTSrILfqSGIG
ChainResidueDetails
AGLY467-GLY481

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1076
DetailsRegion: {"description":"Oxidoreductase"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"E4QP00","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues58
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 12493734
ChainResidueDetails
AHIS689
AASN732

site_idCSA2
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 12493734
ChainResidueDetails
BHIS689
BASN732

site_idMCSA1
Number of Residues3
DetailsM-CSA 673
ChainResidueDetails
ATYR609activator, electrostatic stabiliser, hydrogen bond donor
AHIS689electrostatic stabiliser, proton acceptor, proton donor
AASN732activator, electrostatic stabiliser, enhance reactivity

site_idMCSA2
Number of Residues3
DetailsM-CSA 673
ChainResidueDetails
BTYR609activator, electrostatic stabiliser, hydrogen bond donor
BHIS689electrostatic stabiliser, proton acceptor, proton donor
BASN732activator, electrostatic stabiliser, enhance reactivity

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PDB entries from 2025-08-27

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