1CEL

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

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
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0005975	biological_process	carbohydrate metabolic process

Functional Information from PDB Data

site_id	CAA
Number of Residues	5
Details

Chain	Residue
A	GLU295
A	GLU325
B	GLU295
B	GLU325
A	HOH705

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site_id	CTA
Number of Residues	4
Details

Chain	Residue
A	GLU212
A	ASP214
A	GLU217
A	HIS228

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site_id	CTB
Number of Residues	4
Details

Chain	Residue
B	GLU212
B	ASP214
B	GLU217
B	HIS228

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	72
Details	Compositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"24341799","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8036495","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"24341799","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8036495","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	2
Details	Site: {"description":"Not glycosylated","evidences":[{"source":"PubMed","id":"9746354","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc) asparagine","evidences":[{"source":"PubMed","id":"9746354","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI6
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc) asparagine","evidences":[{"source":"PubMed","id":"24341799","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8036495","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9466911","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9746354","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI7
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc) asparagine","evidences":[{"source":"PubMed","id":"24341799","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9466911","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9746354","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 8036495

Chain	Residue	Details
A	GLU212
A	HIS228
A	ASP214
A	GLU217

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site_id	CSA2
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 8036495

Chain	Residue	Details
B	GLU212
B	HIS228
B	ASP214
B	GLU217

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site_id	MCSA1
Number of Residues	4
Details	M-CSA 444

Chain	Residue	Details
A	TRP216	covalent catalysis
A	ALA218	modifies pKa
A	ILE221	proton shuttle (general acid/base)
A	THR232	modifies pKa

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site_id	MCSA2
Number of Residues	4
Details	M-CSA 444

Chain	Residue	Details
B	TRP216	covalent catalysis
B	ALA218	modifies pKa
B	ILE221	proton shuttle (general acid/base)
B	THR232	modifies pKa

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