3PZV

C2 crystal form of the endo-1,4-beta-glucanase from Bacillus subtilis 168

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000272	biological_process	polysaccharide catabolic process
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0005975	biological_process	carbohydrate metabolic process
B	0000272	biological_process	polysaccharide catabolic process
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0005975	biological_process	carbohydrate metabolic process
C	0000272	biological_process	polysaccharide catabolic process
C	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
C	0005975	biological_process	carbohydrate metabolic process
D	0000272	biological_process	polysaccharide catabolic process
D	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
D	0005975	biological_process	carbohydrate metabolic process

Functional Information from PROSITE/UniProt

site_id	PS00659
Number of Residues	10
Details	GLYCOSYL_HYDROL_F5 Glycosyl hydrolases family 5 signature. VIYEIANEPN

Chain	Residue	Details
A	VAL162-ASN171

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"O85465","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"O85465","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"O85465","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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