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2DEP

Crystal Structure of xylanase B from Clostridium stercorarium F9

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008810molecular_functioncellulase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030245biological_processcellulose catabolic process
A0031176molecular_functionendo-1,4-beta-xylanase activity
A0045493biological_processxylan catabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0008810molecular_functioncellulase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0030245biological_processcellulose catabolic process
B0031176molecular_functionendo-1,4-beta-xylanase activity
B0045493biological_processxylan catabolic process
Functional Information from PROSITE/UniProt
site_idPS00591
Number of Residues11
DetailsGH10_1 Glycosyl hydrolases family 10 (GH10) active site. GLDNiITELDM
ChainResidueDetails
AGLY286-MET296

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AGLU185
BGLU185

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10061
ChainResidueDetails
AGLU293
BGLU293

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1exp
ChainResidueDetails
AHIS264
AGLU185
AGLU293
AASP295

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1exp
ChainResidueDetails
BHIS264
BGLU185
BGLU293
BASP295

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1exp
ChainResidueDetails
AGLU185

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1exp
ChainResidueDetails
BGLU185

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PDB entries from 2024-07-17

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