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4XQW

X-ray structure analysis of xylanase-N44E with MES at pH6.0

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 PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue IOD A 201
ChainResidue
AASN82
ASER146

site_idAC2
Number of Residues2
Detailsbinding site for residue IOD A 203
ChainResidue
ATHR2
AMET169

site_idAC3
Number of Residues2
Detailsbinding site for residue IOD A 204
ChainResidue
AVAL123
AGLN125

site_idAC4
Number of Residues2
Detailsbinding site for residue IOD A 205
ChainResidue
APRO68
AGLY70

site_idAC5
Number of Residues11
Detailsbinding site for residue MES A 206
ChainResidue
AVAL46
ATYR73
ATYR77
AGLU86
ATYR88
AARG122
AGLN136
ATRP138
AGLU177
AHOH390
AGLU44

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
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:26392527, ECO:0000305|PubMed:24419374
ChainResidueDetails
ATYR87

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:26392527, ECO:0000305|PubMed:24419374
ChainResidueDetails
AGLY178

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:24419374
ChainResidueDetails
ALEU74
AGLY78
AILE89
AVAL123
ASER127
ATYR137
AGLN172

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:1369024, ECO:0000269|PubMed:16790934
ChainResidueDetails
ATHR2

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
ATRP39
APHE62

225158

PDB entries from 2024-09-18

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