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1QH6

CATALYSIS AND SPECIFICITY IN ENZYMATIC GLYCOSIDE HYDROLASES: A 2,5B CONFORMATION FOR THE GLYCOSYL-ENZYME INTERMIDIATE REVEALED BY THE STRUCTURE OF THE BACILLUS AGARADHAERENS FAMILY 11 XYLANASE

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_idACA
Number of Residues1
DetailsCATALYTIC ACID / BASE
ChainResidue
AGLU184

site_idACB
Number of Residues1
DetailsCATALYTIC ACID / BASE
ChainResidue
BGLU184

site_idNUA
Number of Residues1
DetailsCATALYTIC NUCLEOPHILE
ChainResidue
AGLU94

site_idNUB
Number of Residues1
DetailsCATALYTIC NUCLEOPHILE
ChainResidue
BGLU94

Functional Information from PROSITE/UniProt
site_idPS00776
Number of Residues11
DetailsGH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLvEYYIVDsW
ChainResidueDetails
APRO91-TRP101

site_idPS00777
Number of Residues12
DetailsGH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. LtvEGYQSSGsA
ChainResidueDetails
ALEU181-ALA192

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bvv
ChainResidueDetails
AGLU184
AGLU94

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bvv
ChainResidueDetails
BGLU184
BGLU94

219140

PDB entries from 2024-05-01

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