1L2A

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0005975	biological_process	carbohydrate metabolic process
A	0008810	molecular_function	cellulase activity
A	0030245	biological_process	cellulose catabolic process
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0005975	biological_process	carbohydrate metabolic process
B	0008810	molecular_function	cellulase activity
B	0030245	biological_process	cellulose catabolic process
C	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
C	0005975	biological_process	carbohydrate metabolic process
C	0008810	molecular_function	cellulase activity
C	0030245	biological_process	cellulose catabolic process
D	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
D	0005975	biological_process	carbohydrate metabolic process
D	0008810	molecular_function	cellulase activity
D	0030245	biological_process	cellulose catabolic process
E	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
E	0005975	biological_process	carbohydrate metabolic process
E	0008810	molecular_function	cellulase activity
E	0030245	biological_process	cellulose catabolic process
F	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
F	0005975	biological_process	carbohydrate metabolic process
F	0008810	molecular_function	cellulase activity
F	0030245	biological_process	cellulose catabolic process

Functional Information from PROSITE/UniProt

site_id	PS00430
Number of Residues	78
Details	TONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. mvksrkisillavamlvsimipttafagptkaptkdgtsykdlflelygkikdpkngyfspdegipyhsi.............................................ETLIVEAP

Chain	Residue	Details
A	MET1-PRO78

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: Proton donor => ECO:0000269\|PubMed:20967294

site_id	SWS_FT_FI2
Number of Residues	6
Details	ACT_SITE: Nucleophile => ECO:0000269\|PubMed:20967294