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3LGR

Xylanase II from Trichoderma reesei cocrystallized with tris-dipicolinate europium

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 Residues6
DetailsBINDING SITE FOR RESIDUE EU A 201
ChainResidue
APDC302
APDC302
APDC303
APDC303
APDC304
APDC304

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EU A 202
ChainResidue
AHOH229

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EU A 203
ChainResidue
AHOH331
AHOH544

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PDC A 302
ChainResidue
AGLN4
APRO5
AASN19
AGLY21
AHIS22
AGLY23
AGLY23
AGLY24
AEU201
AEU201
APDC303
APDC303
APDC304
APDC304
AHOH383
AHOH514

site_idAC5
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PDC A 303
ChainResidue
AGLN4
APRO5
AASN19
AGLY21
AHIS22
AGLY23
AGLY24
AEU201
AEU201
APDC302
APDC302
APDC304
APDC304
AHOH383
AHOH514

site_idAC6
Number of Residues18
DetailsBINDING SITE FOR RESIDUE PDC A 304
ChainResidue
AILE3
AILE3
AGLN4
AGLN4
ATYR17
ATYR17
AVAL25
AVAL25
AEU201
AEU201
APDC302
APDC302
APDC303
APDC303
AHOH351
AHOH351
AHOH395
AHOH395

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

249697

PDB entries from 2026-02-25

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