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1JV1

CRYSTAL STRUCTURE OF HUMAN AGX1 COMPLEXED WITH UDPGLCNAC

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 Residues28
DetailsBINDING SITE FOR RESIDUE UD1 A 901
ChainResidue
ALEU108
AVAL252
AVAL289
AGLY290
AGLU303
ATYR304
AASN327
APHE381
APHE383
APHE403
ALYS407
AGLY110
AHOH908
AHOH929
AHOH946
AHOH1023
AHOH1080
AHOH1358
BARG453
BLYS455
BHOH1268
AGLY111
AMET165
AGLN196
APRO220
AGLY222
AASN223
ACYS251

site_idAC2
Number of Residues26
DetailsBINDING SITE FOR RESIDUE UD1 B 902
ChainResidue
ALYS455
BLEU108
BGLY110
BGLY111
BMET165
BGLN196
BPRO220
BGLY222
BASN223
BCYS251
BVAL252
BVAL289
BGLY290
BGLU303
BTYR304
BASN327
BPHE381
BPHE383
BPHE403
BLYS407
BHOH905
BHOH918
BHOH1082
BHOH1086
BHOH1234
BHOH1269

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
ATYR472
BCYS251
BTYR472

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

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PDB entries from 2024-07-17

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