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2DCZ

Thermal Stabilization of Bacillus subtilis Family-11 Xylanase By Directed Evolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031176molecular_functionendo-1,4-beta-xylanase activity
A0045493biological_processxylan catabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0031176molecular_functionendo-1,4-beta-xylanase activity
B0045493biological_processxylan catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 201
ChainResidue
ASER74
ALEU76
ATHR93
ATHR109
ATHR111
AHOH316
AHOH326
AHOH353

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DIO A 301
ChainResidue
AALA18
BVAL19
BGLY21
AVAL16

Functional Information from PROSITE/UniProt
site_idPS00776
Number of Residues11
DetailsGH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLiEYYVVDsW
ChainResidueDetails
APRO75-TRP85

site_idPS00777
Number of Residues12
DetailsGH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. MatEGYQSSGcS
ChainResidueDetails
AMET169-SER180

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10062, ECO:0000269|PubMed:7911679
ChainResidueDetails
AGLU78
BGLU78

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10063
ChainResidueDetails
AGLU172
BGLU172

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bvv
ChainResidueDetails
AGLU172
AGLU78

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bvv
ChainResidueDetails
BGLU172
BGLU78

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PDB entries from 2024-07-31

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