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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
A0016787molecular_functionhydrolase activity
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
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10064","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10064","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

248335

PDB entries from 2026-01-28

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