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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
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:O85465
ChainResidueDetails
AGLU169
BGLU169

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:O85465
ChainResidueDetails
AGLU257
BGLU257

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:O85465
ChainResidueDetails
AHIS65
BTRP69
BTYR96
BHIS131
BTYR231
BALA263
BTRP291
BLYS296
ATRP69
ATYR96
AHIS131
ATYR231
AALA263
ATRP291
ALYS296
BHIS65

225946

PDB entries from 2024-10-09

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