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2B46

Crystal structure of an engineered uninhibited Bacillus subtilis xylanase in substrate bound state

Functional Information from GO Data
ChainGOidnamespacecontents
X0000272biological_processpolysaccharide catabolic process
X0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
X0005975biological_processcarbohydrate metabolic process
X0016787molecular_functionhydrolase activity
X0016798molecular_functionhydrolase activity, acting on glycosyl bonds
X0031176molecular_functionendo-1,4-beta-xylanase activity
X0045493biological_processxylan catabolic process
Functional Information from PROSITE/UniProt
site_idPS00776
Number of Residues11
DetailsGH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLiEYYVVDsW
ChainResidueDetails
XPRO75-TRP85

site_idPS00777
Number of Residues12
DetailsGH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. MatEGYQSSGsS
ChainResidueDetails
XMET169-SER180

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10062, ECO:0000269|PubMed:7911679
ChainResidueDetails
XGLU78

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10063
ChainResidueDetails
XGLU172

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bvv
ChainResidueDetails
XGLU172
XGLU78

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PDB entries from 2025-06-18

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