7CEL

CBH1 (E217Q) IN COMPLEX WITH CELLOHEXAOSE AND CELLOBIOSE

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

Functional Information from PDB Data

site_id	CAT
Number of Residues	4
Details	CATALYTIC SITE INCLUDING MUTATION E217Q.

Chain	Residue
A	GLU212
A	ASP214
A	GLN217
A	HIS228

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site_id	COB
Number of Residues	3
Details	COBALT-BINDING SITE ON CRYSTALLOGRAPHIC DYAD. THE METAL ION IS BOUND BY GLU 295 AND GLU 325 FROM TWO CRYSTALLOGRAPHICALLY RELATED MOLECULES.

Chain	Residue
A	GLU295
A	GLU325
A	CO1000

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: ACT_SITE => ECO:0000250

Chain	Residue	Details
A	GLU126

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:24341799, ECO:0000305|PubMed:8036495

Chain	Residue	Details
A	GLU212

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site_id	SWS_FT_FI3
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:24341799, ECO:0000305|PubMed:8036495

Chain	Residue	Details
A	GLN217

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site_id	SWS_FT_FI4
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc) asparagine => ECO:0000269|PubMed:9746354

Chain	Residue	Details
A	ASN45

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site_id	SWS_FT_FI5
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN64

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site_id	SWS_FT_FI6
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc) asparagine => ECO:0000269|PubMed:24341799, ECO:0000269|PubMed:8036495, ECO:0000269|PubMed:9466911, ECO:0000269|PubMed:9746354

Chain	Residue	Details
A	ASN270

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site_id	SWS_FT_FI7
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc) asparagine => ECO:0000269|PubMed:24341799, ECO:0000269|PubMed:9466911, ECO:0000269|PubMed:9746354

Chain	Residue	Details
A	ASN384

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site_id	SWS_FT_FI8
Number of Residues	1
Details	SITE: Not glycosylated => ECO:0000269|PubMed:9746354

Chain	Residue	Details
A	ASN64

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site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|DOI:10.1016/0014-5793(80)81006-4, ECO:0000269|DOI:10.1038/nbt1083-687, ECO:0007744|PDB:1EGN, ECO:0007744|PDB:1Q2B, ECO:0007744|PDB:1Q2E

Chain	Residue	Details
A	PCA1

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1cel

Chain	Residue	Details
A	GLU212
A	HIS228
A	ASP214
A	GLN217

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site_id	MCSA1
Number of Residues	4
Details	M-CSA 444

Chain	Residue	Details
A	GLU212	covalent catalysis
A	ASP214	modifies pKa
A	GLN217	proton shuttle (general acid/base)
A	HIS228	modifies pKa

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