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3O5S

Crystal Structure of the endo-beta-1,3-1,4 glucanase from Bacillus subtilis (strain 168)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0042972molecular_functionlicheninase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 243
ChainResidue
APRO37
AGLY73
AASP235
AHOH414
AHOH419

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE B3P A 244
ChainResidue
ATRP220
AHOH337
AHOH344
ATRP131
AGLU133
AGLU137
ATYR151

Functional Information from PROSITE/UniProt
site_idPS01034
Number of Residues11
DetailsGH16_1 Glycosyl hydrolases family 16 active sites. EIDI.EflGKdT
ChainResidueDetails
AGLU133-THR143

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10064
ChainResidueDetails
AGLU133

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10064
ChainResidueDetails
AGLU137

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|Ref.7
ChainResidueDetails
AGLN29

227344

PDB entries from 2024-11-13

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