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3AKP

Crystal structure of xylanase from Trichoderma longibrachiatum

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031176molecular_functionendo-1,4-beta-xylanase activity
A0045493biological_processxylan catabolic process
A0046872molecular_functionmetal ion binding
B0000272biological_processpolysaccharide catabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0031176molecular_functionendo-1,4-beta-xylanase activity
B0045493biological_processxylan catabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 191
ChainResidue
ATRP18
AHOH310
AHOH424
AASN44
AGLU86
ATYR88
AGLU177
AGOL192
AHOH207
AHOH212
AHOH264

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 192
ChainResidue
ATYR77
ATYR171
AGOL191
AHOH208
AHOH310
AHOH346
AHOH395

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL B 191
ChainResidue
BTRP18
BASN44
BGLU86
BTYR88
BGLU177
BHOH198
BHOH229
BHOH340
BHOH422
BHOH423

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

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PDB entries from 2025-12-03

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