Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1VM8

Crystal structure of UDP-N-acetylglucosamine pyrophosphorylase (Agx2) from Mus musculus at 2.50 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0002376biological_processimmune system process
A0003977molecular_functionUDP-N-acetylglucosamine diphosphorylase activity
A0005654cellular_componentnucleoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006047biological_processUDP-N-acetylglucosamine metabolic process
A0006048biological_processUDP-N-acetylglucosamine biosynthetic process
A0016740molecular_functiontransferase activity
A0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
A0016779molecular_functionnucleotidyltransferase activity
A0030246molecular_functioncarbohydrate binding
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
B0005654cellular_componentnucleoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006047biological_processUDP-N-acetylglucosamine metabolic process
B0006048biological_processUDP-N-acetylglucosamine biosynthetic process
B0016740molecular_functiontransferase activity
B0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
B0016779molecular_functionnucleotidyltransferase activity
B0030246molecular_functioncarbohydrate binding
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 Residues3
DetailsBINDING SITE FOR RESIDUE CL B 523
ChainResidue
BARG9
BASN41
BPHE42

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 524
ChainResidue
BARG422
BHIS423

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 525
ChainResidue
BLYS180

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 526
ChainResidue
BGLU502
BHOH552

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 523
ChainResidue
APHE42
AARG9

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO B 527
ChainResidue
BLYS390

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 528
ChainResidue
BLEU77
BASP83
BLYS271
BHOH584

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues26
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q16222","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

PDB statisticsPDBj update infoContact PDBjnumon