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2VUL

Thermostable mutant of ENVIRONMENTALLY ISOLATED GH11 XYLANASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1195
ChainResidue
AALA2
ALEU6
ATHR7
ASER8
AGLN10

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 1196
ChainResidue
AHOH2182
AHOH2183
AHOH2184
AHOH2185
ATRP55
AGLN56
ATHR57
AHOH2061

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 12P A 1197
ChainResidue
AGLY110
ATHR111
AASN113
AASN158
AALA162
ASER165
AHOH2160
AHOH2186

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 12P A 1198
ChainResidue
AASN85
APRO86
APHE108
AARG123
ATYR139
ATYR141
AGLY167
AHOH2161
AHOH2167
AHOH2187
AHOH2188

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 12P A 1199
ChainResidue
ASER20
AASN48
ATYR80
AGLU89
ATRP99
AILE132
ATYR175
AHOH2130
AHOH2189
AHOH2190
AHOH2191

Functional Information from PROSITE/UniProt
site_idPS00776
Number of Residues11
DetailsGH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLvEYYVVDsW
ChainResidueDetails
APRO86-TRP96

site_idPS00777
Number of Residues12
DetailsGH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. MatEGYQSSGsS
ChainResidueDetails
AMET178-SER189

218853

PDB entries from 2024-04-24

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