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2DFB

Xylanase II from Tricoderma reesei at 100K

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005576cellular_componentextracellular region
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
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 191
ChainResidue
AGLN4
APRO5
AASN19
AHOH220
AHOH244
AHOH267
AHOH285
AHOH290
AHOH452

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD A 192
ChainResidue
AASN82
ASER146

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 193
ChainResidue
AARG119

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 194
ChainResidue
APRO68

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD A 195
ChainResidue
ASER65
ASER184

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD A 196
ChainResidue
AVAL123
AGLN125

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IOD A 197
ChainResidue
AGLY30
AGLN34
ASER36

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
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"26392527","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24419374","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"26392527","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24419374","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24419374","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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 2025-11-05

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