1CEL

THE THREE-DIMENSIONAL CRYSTAL STRUCTURE OF THE CATALYTIC CORE OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Protein Modification Annotation
Structure Motif: Primary M-CSA Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1cela_	All beta proteins	Concanavalin A-like lectins/glucanases	Concanavalin A-like lectins/glucanases	Glycosyl hydrolase family 7 catalytic core	Cellobiohydrolase I (cellulase, Endoglucanase I, CBH1)	Hypocrea jecorina (Trichoderma reesei ) [TaxId: 51453 ],	SCOPe (2.08)
B	d1celb_	All beta proteins	Concanavalin A-like lectins/glucanases	Concanavalin A-like lectins/glucanases	Glycosyl hydrolase family 7 catalytic core	Cellobiohydrolase I (cellulase, Endoglucanase I, CBH1)	Hypocrea jecorina (Trichoderma reesei ) [TaxId: 51453 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Concanavalin A-like lectins/glucanases	8037151	3000120	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Concanavalin A-like lectins/glucanases	8037151	3000120	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Glyco_hydro_7	e1celA1	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Concanavalin A-like lectins/glucanases	F: Glyco_hydro_7	ECOD (1.6)
B	Glyco_hydro_7	e1celB1	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Concanavalin A-like lectins/glucanases	F: Glyco_hydro_7	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.70.100.10	Mainly Beta	Distorted Sandwich	1,4-Beta-D-Glucan Cellobiohydrolase I	Chain A	CATH (4.3.0)
B	2.70.100.10	Mainly Beta	Distorted Sandwich	1,4-Beta-D-Glucan Cellobiohydrolase I	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00840	Glycosyl hydrolase family 7 (Glyco_hydro_7)	Glycosyl hydrolase family 7	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE I	hydrolase activity, acting on glycosyl bonds cellulose 1,4-beta-cellobiosidase activity hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity catalytic activity binding polysaccharide binding cellulose binding carbohydrate binding	carbohydrate metabolic process catabolic process glucan catabolic process beta-glucan metabolic process carbohydrate catabolic process primary metabolic process macromolecule catabolic process polysaccharide metabolic process glucan metabolic process beta-glucan catabolic process polysaccharide catabolic process metabolic process cellular process cellulose catabolic process carbohydrate metabolic process catabolic process glucan catabolic process beta-glucan metabolic process carbohydrate catabolic process primary metabolic process macromolecule catabolic process polysaccharide metabolic process glucan metabolic process beta-glucan catabolic process polysaccharide catabolic process metabolic process cellular process cellulose catabolic process macromolecule metabolic process cellulose metabolic process	cellular anatomical structure extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR013320	Concanavalin A-like lectin/glucanase domain superfamily	Homologous Superfamily
A, B	IPR000254	Cellulose-binding domain, fungal	Domain
A, B	IPR037019	Glycoside hydrolase family 7, catalytic domain superfamily	Homologous Superfamily
A, B	IPR001722	Glycoside hydrolase, family 7	Family
A, B	IPR035971	Cellulose-binding domain superfamily	Homologous Superfamily

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A, B	PCA	Parent Component: GLN RESID: AA0031 PSI-MOD : 2-pyrrolidone-5-carboxylic acid (Gln) MOD:00040 , 2-pyrrolidone-5-carboxylic acid (Glu) MOD:00420

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	cellulose 1,4-beta-cellobiosidase (non-reducing end) M-CSA #444	Cellobiohydrolase enzymes depolymerise cellulose into its fundamental repeating unit of two glucose molecules (cellobiose). These enzymes are key components of fungal cellulase multienzyme systems; together with randomly-acting endo-1,4-beta-glucanases (which cut internal beta-1,4-glucosidic bonds) they hydrolyse cellulose via a processive mechanism, forming cellobiose as a major product. Cellobiose is then converted by beta-glucosidases to glucose; the latter product may further be fermented to ethanol or other liquid fuels and chemicals. These enzymes suffer from inhibition by this product, which lingers in the enzymes’ active sites and thus delays their catalytic cycles. Cellobiose accumulates over the course of the reaction unless removed by an enzyme such as beta-glucosidase, which cleaves cellobiose yielding two glucose molecules. This entry represents the Glycoside hydrolase, family 7 (GH7).	Defined by 4 residues: GLU:A-212ASP:A-214GLU:A-217HIS:A-228 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.2.1.91 (PDB Primary Data) Search M-CSA Motif + EC 3.2.1.91

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.