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1F5J

CRYSTAL STRUCTURE OF XYNB, A HIGHLY THERMOSTABLE BETA-1,4-XYLANASE FROM DICTYOGLOMUS THERMOPHILUM RT46B.1, AT 1.8 A RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1001
ChainResidue
BASN164
BARG165
BHOH1061
BHOH1121

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1002
ChainResidue
AASN86
BGLY109
BGLN110
BARG165

Functional Information from PROSITE/UniProt
site_idPS00776
Number of Residues11
DetailsGH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLvEFYIVEsW
ChainResidueDetails
APRO87-TRP97

site_idPS00777
Number of Residues12
DetailsGH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. LcvEGYQSSGsA
ChainResidueDetails
ALEU177-ALA188

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PDB entries from 2024-05-01

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