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1UN1

Xyloglucan endotransglycosylase native structure.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005576cellular_componentextracellular region
A0005618cellular_componentcell wall
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0010411biological_processxyloglucan metabolic process
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0016762molecular_functionxyloglucan:xyloglucosyl transferase activity
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030247molecular_functionpolysaccharide binding
A0042546biological_processcell wall biogenesis
A0044042biological_processglucan metabolic process
A0048046cellular_componentapoplast
A0071555biological_processcell wall organization
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005576cellular_componentextracellular region
B0005618cellular_componentcell wall
B0005737cellular_componentcytoplasm
B0005975biological_processcarbohydrate metabolic process
B0010411biological_processxyloglucan metabolic process
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0016762molecular_functionxyloglucan:xyloglucosyl transferase activity
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0030247molecular_functionpolysaccharide binding
B0042546biological_processcell wall biogenesis
B0044042biological_processglucan metabolic process
B0048046cellular_componentapoplast
B0071555biological_processcell wall organization
Functional Information from PROSITE/UniProt
site_idPS01034
Number of Residues11
DetailsGH16_1 Glycosyl hydrolases family 16 active sites. EIDF.EflGNrT
ChainResidueDetails
AGLU85-THR95

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|PIRSR:PIRSR005604-1, ECO:0000255|PROSITE-ProRule:PRU10064, ECO:0000305|PubMed:15020748
ChainResidueDetails
AGLU85
BGLU85

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|PIRSR:PIRSR005604-1, ECO:0000255|PROSITE-ProRule:PRU10064, ECO:0000305|PubMed:15020748
ChainResidueDetails
AGLU89
BGLU89

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:15020748, ECO:0007744|PDB:1UMZ
ChainResidueDetails
AGLU89
BASP178
BGLY183
BARG258
AGLN102
AASP112
AASP178
AGLY183
AARG258
BGLU89
BGLN102
BASP112

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Important for catalytic activity => ECO:0000305|PubMed:15020748
ChainResidueDetails
AASP87
BASP87

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PIRSR:PIRSR005604-2, ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:15020748, ECO:0007744|PDB:1UMZ, ECO:0007744|PDB:1UN1
ChainResidueDetails
AASN93
BASN93

Catalytic Information from CSA
site_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 15020748
ChainResidueDetails
AGLU85
AASP87
AGLU89

site_idMCSA1
Number of Residues3
DetailsM-CSA 826
ChainResidueDetails
AGLU89covalently attached, hydrogen bond acceptor, nucleofuge, nucleophile
ALEU91electrostatic stabiliser, hydrogen bond donor
AASN93proton acceptor, proton donor

site_idMCSA2
Number of Residues3
DetailsM-CSA 826
ChainResidueDetails
BGLU89covalently attached, hydrogen bond acceptor, nucleofuge, nucleophile
BLEU91electrostatic stabiliser, hydrogen bond donor
BASN93proton acceptor, proton donor

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PDB entries from 2025-06-18

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