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1OCB

Structure of the wild-type cellobiohydrolase Cel6A from Humicolas insolens in complex with a fluorescent substrate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0030245biological_processcellulose catabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0030245biological_processcellulose catabolic process
Functional Information from PROSITE/UniProt
site_idPS00655
Number of Residues17
DetailsGLYCOSYL_HYDROL_F6_1 Glycosyl hydrolases family 6 signature 1. VvYdlPdRDCAaaASnG
ChainResidueDetails
AVAL172-GLY188

site_idPS00656
Number of Residues10
DetailsGLYCOSYL_HYDROL_F6_2 Glycosyl hydrolases family 6 signature 2. ILVIEPDSLA
ChainResidueDetails
AILE220-ALA229

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues44
DetailsRegion: {"description":"Substrate binding loop 1","evidences":[{"source":"PubMed","id":"10413461","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12454501","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12842048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues76
DetailsRegion: {"description":"Substrate binding loop 2","evidences":[{"source":"PubMed","id":"10413461","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12454501","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12842048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10057","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10413461","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12842048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10056","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10413461","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12454501","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12842048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10413461","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12454501","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12842048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsGlycosylation: {"description":"O-linked (Man...) threonine","evidences":[{"source":"PubMed","id":"9882628","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsGlycosylation: {"description":"O-linked (Man...) serine","evidences":[{"source":"PubMed","id":"9882628","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10413461","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12454501","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12842048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9882628","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1qk2
ChainResidueDetails
AARG179
AASP226
AASP180
ATYR174

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1qk2
ChainResidueDetails
BARG179
BASP226
BASP180
BTYR174

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1qk2
ChainResidueDetails
AASP226
AASP405

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1qk2
ChainResidueDetails
BASP226
BASP405

243083

PDB entries from 2025-10-15

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