1OC6

structure native of the D405N mutant of the CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS at 1.5 angstrom resolution

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	0030245	biological_process	cellulose catabolic process

Functional Information from PROSITE/UniProt

site_id	PS00655
Number of Residues	17
Details	GLYCOSYL_HYDROL_F6_1 Glycosyl hydrolases family 6 signature 1. VvYdlPdRDCAaaASnG

Chain	Residue	Details
A	VAL172-GLY188

site_id	PS00656
Number of Residues	10
Details	GLYCOSYL_HYDROL_F6_2 Glycosyl hydrolases family 6 signature 2. ILVIEPDSLA

Chain	Residue	Details
A	ILE220-ALA229

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	22
Details	Region: {"description":"Substrate binding loop 1","evidences":[{"source":"PubMed","id":"10413461","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12454501","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12842048","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	38
Details	Region: {"description":"Substrate binding loop 2","evidences":[{"source":"PubMed","id":"10413461","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12454501","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12842048","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10057","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10413461","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12842048","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10056","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10413461","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12454501","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12842048","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10413461","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12454501","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12842048","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Glycosylation: {"description":"O-linked (Man...) threonine","evidences":[{"source":"PubMed","id":"9882628","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Glycosylation: {"description":"O-linked (Man...) serine","evidences":[{"source":"PubMed","id":"9882628","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10413461","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12454501","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12842048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9882628","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1qk2

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1qk2