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3AKQ

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
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ZN A 191
ChainResidue
AHIS144
AHOH349
AZN193
AZN194
AZN195
ACL196
ACL197
AHOH343
AHOH344
AHOH347

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ZN A 192
ChainResidue
AHIS22
AZN193
AZN194
AZN195
ACL197
AHOH346
AHOH348

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ZN A 193
ChainResidue
AZN191
AZN192
ACL196
AHOH345
AHOH347
AHOH348
AHOH349

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 194
ChainResidue
AZN191
AZN192
ACL196
ACL197
AHOH346
AHOH349

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 195
ChainResidue
AZN191
AZN192
ACL197
AHOH344
AHOH350

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CL A 196
ChainResidue
AHIS144
AZN191
AZN193
AZN194
ACL197
AHOH344
AHOH347
AHOH349
AHOH416

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CL A 197
ChainResidue
AZN191
AZN192
AZN194
AZN195
ACL196
AHOH337
AHOH344
AHOH346

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

246031

PDB entries from 2025-12-10

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