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1XND

HIGH-RESOLUTION STRUCTURES OF XYLANASES FROM B. CIRCULANS AND T. HARZIANUM IDENTIFY A NEW FOLDING PATTERN AND IMPLICATIONS FOR THE ATOMIC BASIS OF THE CATALYSIS

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
Functional Information from PDB Data
site_idAS1
Number of Residues2
DetailsCATALYTIC ACIDIC RESIDUES
ChainResidue
AGLU86
AGLU177

site_idAS2
Number of Residues4
DetailsGROUP OF TYROSINE RESIDUES IN THE ACTIVE SITE THAT APPEAR TO BE IMPORTANT FOR SUBSTRATE BINDING
ChainResidue
ATYR14
ATYR77
ATYR88
ATYR171

Functional Information from PROSITE/UniProt
site_idPS00776
Number of Residues11
DetailsGH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLiEYYIVEnF
ChainResidueDetails
APRO83-PHE93

site_idPS00777
Number of Residues12
DetailsGH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. VavEGYFSSGsA
ChainResidueDetails
AVAL174-ALA185

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile
ChainResidueDetails
AGLU86

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor
ChainResidueDetails
AGLU177

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bvv
ChainResidueDetails
AGLU177
AGLU86

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PDB entries from 2024-11-06

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