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1JVG

CRYSTAL STRUCTURE OF HUMAN AGX2 COMPLEXED WITH UDPGALNAC

Functional Information from GO Data
ChainGOidnamespacecontents
A0002376biological_processimmune system process
A0003977molecular_functionUDP-N-acetylglucosamine diphosphorylase activity
A0005829cellular_componentcytosol
A0006048biological_processUDP-N-acetylglucosamine biosynthetic process
A0016740molecular_functiontransferase activity
A0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
A0016779molecular_functionnucleotidyltransferase activity
A0032481biological_processpositive regulation of type I interferon production
A0042802molecular_functionidentical protein binding
A0045087biological_processinnate immune response
A0052630molecular_functionUDP-N-acetylgalactosamine diphosphorylase activity
A0070569molecular_functionuridylyltransferase activity
A0140374biological_processantiviral innate immune response
A0141090molecular_functionprotein serine pyrophosphorylase activity
B0002376biological_processimmune system process
B0003977molecular_functionUDP-N-acetylglucosamine diphosphorylase activity
B0005829cellular_componentcytosol
B0006048biological_processUDP-N-acetylglucosamine biosynthetic process
B0016740molecular_functiontransferase activity
B0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
B0016779molecular_functionnucleotidyltransferase activity
B0032481biological_processpositive regulation of type I interferon production
B0042802molecular_functionidentical protein binding
B0045087biological_processinnate immune response
B0052630molecular_functionUDP-N-acetylgalactosamine diphosphorylase activity
B0070569molecular_functionuridylyltransferase activity
B0140374biological_processantiviral innate immune response
B0141090molecular_functionprotein serine pyrophosphorylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues26
DetailsBINDING SITE FOR RESIDUE UD2 A 1901
ChainResidue
ALEU108
AVAL252
AGLY290
AGLU303
ATYR304
AASN327
AILE328
AALA329
APHE381
APHE383
ALYS407
AGLY110
AHOH1925
AHOH1957
AHOH1996
AHOH2046
AHOH2047
AHOH2049
BARG453
AGLY111
AMET165
AGLN196
APRO220
AGLY222
AASN223
ACYS251

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE UD2 B 1902
ChainResidue
AARG453
BLEU108
BGLY110
BGLY111
BMET165
BGLN196
BPRO220
BGLY222
BASN223
BCYS251
BVAL252
BGLY290
BGLU303
BTYR304
BASN327
BILE328
BALA329
BPHE383
BLYS407
BHOH1914
BHOH1936

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues22
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11707391","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JV1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1JVD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11707391","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JV1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11707391","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JVD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PDB","id":"1JV1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1JVD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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