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3AKR

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
A0008152biological_processmetabolic 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
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 191
ChainResidue
ATRP18
AASN44
AGLU86
ATYR88
AGLU177
AHOH218
AHOH344
AHOH384
AHOH418

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 192
ChainResidue
AASN124
AGLN125
AHOH273
AHOH309
AHOH370
AHOH395

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 193
ChainResidue
AASN92
APHE93
AHIS144
AHOH224
AHOH231
AHOH270

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

217705

PDB entries from 2024-03-27

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