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3D6E

Crystal structure of the engineered 1,3-1,4-beta-glucanase protein from Bacillus licheniformis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0042972molecular_functionlicheninase activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0042972molecular_functionlicheninase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 202
ChainResidue
APRO9
AGLY32
AASN194
AHOH227
AHOH260

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA B 202
ChainResidue
BPRO9
BGLY32
BASN194

Functional Information from PROSITE/UniProt
site_idPS01034
Number of Residues11
DetailsGH16_1 Glycosyl hydrolases family 16 active sites. EIDI.EflGKdT
ChainResidueDetails
AGLU92-THR102

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile
ChainResidueDetails
AVAL105
BVAL105

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor
ChainResidueDetails
ATYR109
BTYR109

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 2ayh
ChainResidueDetails
AGLU92
AGLU96
AASP94

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 2ayh
ChainResidueDetails
BGLU92
BGLU96
BASP94

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PDB entries from 2025-06-18

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