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4XQ4

X-ray structure analysis of xylanase - N44D

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0008152biological_processmetabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031176molecular_functionendo-1,4-beta-xylanase activity
A0045493biological_processxylan catabolic process
B0000272biological_processpolysaccharide catabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005576cellular_componentextracellular region
B0005975biological_processcarbohydrate metabolic process
B0008152biological_processmetabolic process
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0031176molecular_functionendo-1,4-beta-xylanase activity
B0045493biological_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 202
ChainResidue
ASER65
ASER184

site_idAC3
Number of Residues2
Detailsbinding site for residue IOD B 201
ChainResidue
BASN82
BSER146

site_idAC4
Number of Residues2
Detailsbinding site for residue IOD B 202
ChainResidue
BASN67
BSER184

site_idAC5
Number of Residues4
Detailsbinding site for residue IOD B 203
ChainResidue
BTHR26
BASN38
BHOH514
BGLY24

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 Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:26392527, ECO:0000305|PubMed:24419374
ChainResidueDetails
ATYR87
BTYR87

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:26392527, ECO:0000305|PubMed:24419374
ChainResidueDetails
AGLY178
BGLY178

site_idSWS_FT_FI3
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:24419374
ChainResidueDetails
ALEU74
BILE89
BVAL123
BSER127
BTYR137
BGLN172
AGLY78
AILE89
AVAL123
ASER127
ATYR137
AGLN172
BLEU74
BGLY78

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:1369024, ECO:0000269|PubMed:16790934
ChainResidueDetails
ATHR2
BTHR2

site_idSWS_FT_FI5
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
ATRP39
APHE62
BTRP39
BPHE62

218853

PDB entries from 2024-04-24

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