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6KWH

Crystal Structure Analysis of Endo-beta-1,4-xylanase II Complexed with Xylotriose

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031176molecular_functionendo-1,4-beta-xylanase activity
A0045493biological_processxylan catabolic process
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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:26392527, ECO:0000305|PubMed:24419374
ChainResidueDetails
AGLU86

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:26392527, ECO:0000305|PubMed:24419374
ChainResidueDetails
AASN177

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:24419374
ChainResidueDetails
ATYR171
ATYR73
ATYR77
ATYR88
AARG122
APRO126
AGLN136

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN61
AASN38

221051

PDB entries from 2024-06-12

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