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1L2A

The Crystal Structure and Catalytic Mechanism of Cellobiohydrolase CelS, the Major Enzymatic Component of the Clostridium thermocellum cellulosome

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008810molecular_functioncellulase activity
A0030245biological_processcellulose catabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0008810molecular_functioncellulase activity
B0030245biological_processcellulose catabolic process
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0005975biological_processcarbohydrate metabolic process
C0008810molecular_functioncellulase activity
C0030245biological_processcellulose catabolic process
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0005975biological_processcarbohydrate metabolic process
D0008810molecular_functioncellulase activity
D0030245biological_processcellulose catabolic process
E0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
E0005975biological_processcarbohydrate metabolic process
E0008810molecular_functioncellulase activity
E0030245biological_processcellulose catabolic process
F0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
F0005975biological_processcarbohydrate metabolic process
F0008810molecular_functioncellulase activity
F0030245biological_processcellulose catabolic process
Functional Information from PROSITE/UniProt
site_idPS00430
Number of Residues78
DetailsTONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. mvksrkisillavamlvsimipttafagptkaptkdgtsykdlflelygkikdpkngyfspdegipyhsi.............................................ETLIVEAP
ChainResidueDetails
AMET1-PRO78

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"20967294","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"20967294","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues42
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12096911","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues24
DetailsBinding site: {}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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