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3AKT

Crystal structure of xylanase from Trichoderma longibrachiatum

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
A0046872molecular_functionmetal ion binding
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
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 191
ChainResidue
ATRP18
AHOH293
AHOH344
AASN44
AGLU86
ATYR88
AGLU177
AGOL192
AHOH198
AHOH218
AHOH247

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 192
ChainResidue
ATYR77
ATYR171
AGOL191
AHOH213
AHOH247
AHOH276
AHOH308

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL B 191
ChainResidue
BTRP18
BASN44
BGLU86
BTYR88
BGLU177
BHOH234
BHOH278
BHOH286
BHOH302
BHOH397

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 2024-11-06

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