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1JVG

CRYSTAL STRUCTURE OF HUMAN AGX2 COMPLEXED WITH UDPGALNAC

Functional Information from GO Data
ChainGOidnamespacecontents
A0003977molecular_functionUDP-N-acetylglucosamine diphosphorylase activity
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006048biological_processUDP-N-acetylglucosamine biosynthetic process
A0016740molecular_functiontransferase activity
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
B0003977molecular_functionUDP-N-acetylglucosamine diphosphorylase activity
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006048biological_processUDP-N-acetylglucosamine biosynthetic process
B0016740molecular_functiontransferase activity
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: BINDING => ECO:0000269|PubMed:11707391, ECO:0007744|PDB:1JV1, ECO:0007744|PDB:1JVD
ChainResidueDetails
ALEU108
ATYR304
AASN327
BLEU108
BGLY110
BGLY111
BGLN196
BGLY222
BASN223
BVAL252
BGLY290
AGLY110
BGLU303
BTYR304
BASN327
AGLY111
AGLN196
AGLY222
AASN223
AVAL252
AGLY290
AGLU303

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:11707391, ECO:0007744|PDB:1JV1
ChainResidueDetails
ACYS251
ALYS472
BCYS251
BLYS472

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:11707391, ECO:0007744|PDB:1JVD
ChainResidueDetails
APHE381
BPHE381

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:1JV1, ECO:0007744|PDB:1JVD
ChainResidueDetails
ALYS407
BLYS407

226707

PDB entries from 2024-10-30

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