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3PZU

P212121 crystal form of the endo-1,4-beta-glucanase from Bacillus subtilis 168

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
B0000272biological_processpolysaccharide catabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 1
ChainResidue
AALA37
BGLN297
ALYS38
AGLY306
AALA307
ASER308
ATRP313
AHOH438
AHOH501
BLYS296

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 1
ChainResidue
AGLN48
AALA56
ATHR285
BTRP207
BGLN209
BHIS235
BHOH343
BHOH360

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 333
ChainResidue
APRO35
AASN39
ATHR89
AHOH401
BASP262
BSER264
BHOH490

Functional Information from PROSITE/UniProt
site_idPS00659
Number of Residues10
DetailsGLYCOSYL_HYDROL_F5 Glycosyl hydrolases family 5 signature. VIYEIANEPN
ChainResidueDetails
AVAL162-ASN171

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"O85465","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"O85465","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"O85465","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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