1JVG
CRYSTAL STRUCTURE OF HUMAN AGX2 COMPLEXED WITH UDPGALNAC
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003977 | molecular_function | UDP-N-acetylglucosamine diphosphorylase activity |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0006048 | biological_process | UDP-N-acetylglucosamine biosynthetic process |
A | 0016740 | molecular_function | transferase activity |
A | 0016779 | molecular_function | nucleotidyltransferase activity |
A | 0032481 | biological_process | positive regulation of type I interferon production |
A | 0042802 | molecular_function | identical protein binding |
A | 0045087 | biological_process | innate immune response |
A | 0052630 | molecular_function | UDP-N-acetylgalactosamine diphosphorylase activity |
A | 0070569 | molecular_function | uridylyltransferase activity |
A | 0140374 | biological_process | antiviral innate immune response |
A | 0141090 | molecular_function | protein serine pyrophosphorylase activity |
B | 0003977 | molecular_function | UDP-N-acetylglucosamine diphosphorylase activity |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0005886 | cellular_component | plasma membrane |
B | 0006048 | biological_process | UDP-N-acetylglucosamine biosynthetic process |
B | 0016740 | molecular_function | transferase activity |
B | 0016779 | molecular_function | nucleotidyltransferase activity |
B | 0032481 | biological_process | positive regulation of type I interferon production |
B | 0042802 | molecular_function | identical protein binding |
B | 0045087 | biological_process | innate immune response |
B | 0052630 | molecular_function | UDP-N-acetylgalactosamine diphosphorylase activity |
B | 0070569 | molecular_function | uridylyltransferase activity |
B | 0140374 | biological_process | antiviral innate immune response |
B | 0141090 | molecular_function | protein serine pyrophosphorylase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE UD2 A 1901 |
Chain | Residue |
A | LEU108 |
A | VAL252 |
A | GLY290 |
A | GLU303 |
A | TYR304 |
A | ASN327 |
A | ILE328 |
A | ALA329 |
A | PHE381 |
A | PHE383 |
A | LYS407 |
A | GLY110 |
A | HOH1925 |
A | HOH1957 |
A | HOH1996 |
A | HOH2046 |
A | HOH2047 |
A | HOH2049 |
B | ARG453 |
A | GLY111 |
A | MET165 |
A | GLN196 |
A | PRO220 |
A | GLY222 |
A | ASN223 |
A | CYS251 |
site_id | AC2 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE UD2 B 1902 |
Chain | Residue |
A | ARG453 |
B | LEU108 |
B | GLY110 |
B | GLY111 |
B | MET165 |
B | GLN196 |
B | PRO220 |
B | GLY222 |
B | ASN223 |
B | CYS251 |
B | VAL252 |
B | GLY290 |
B | GLU303 |
B | TYR304 |
B | ASN327 |
B | ILE328 |
B | ALA329 |
B | PHE383 |
B | LYS407 |
B | HOH1914 |
B | HOH1936 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 22 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11707391, ECO:0007744|PDB:1JV1, ECO:0007744|PDB:1JVD |
Chain | Residue | Details |
A | LEU108 | |
A | TYR304 | |
A | ASN327 | |
B | LEU108 | |
B | GLY110 | |
B | GLY111 | |
B | GLN196 | |
B | GLY222 | |
B | ASN223 | |
B | VAL252 | |
B | GLY290 | |
A | GLY110 | |
B | GLU303 | |
B | TYR304 | |
B | ASN327 | |
A | GLY111 | |
A | GLN196 | |
A | GLY222 | |
A | ASN223 | |
A | VAL252 | |
A | GLY290 | |
A | GLU303 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11707391, ECO:0007744|PDB:1JV1 |
Chain | Residue | Details |
A | CYS251 | |
A | LYS472 | |
B | CYS251 | |
B | LYS472 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11707391, ECO:0007744|PDB:1JVD |
Chain | Residue | Details |
A | PHE381 | |
B | PHE381 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0007744|PDB:1JV1, ECO:0007744|PDB:1JVD |
Chain | Residue | Details |
A | LYS407 | |
B | LYS407 |