1VM8
Crystal structure of UDP-N-acetylglucosamine pyrophosphorylase (Agx2) from Mus musculus at 2.50 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003977 | molecular_function | UDP-N-acetylglucosamine diphosphorylase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006047 | biological_process | UDP-N-acetylglucosamine metabolic process |
| A | 0006048 | biological_process | UDP-N-acetylglucosamine biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0030246 | molecular_function | carbohydrate binding |
| A | 0045087 | biological_process | innate immune response |
| A | 0052630 | molecular_function | UDP-N-acetylgalactosamine diphosphorylase activity |
| A | 0070569 | molecular_function | uridylyltransferase activity |
| A | 0141090 | molecular_function | protein serine pyrophosphorylase activity |
| B | 0003977 | molecular_function | UDP-N-acetylglucosamine diphosphorylase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006047 | biological_process | UDP-N-acetylglucosamine metabolic process |
| B | 0006048 | biological_process | UDP-N-acetylglucosamine biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0030246 | molecular_function | carbohydrate binding |
| B | 0045087 | biological_process | innate immune response |
| B | 0052630 | molecular_function | UDP-N-acetylgalactosamine diphosphorylase activity |
| B | 0070569 | molecular_function | uridylyltransferase activity |
| B | 0141090 | molecular_function | protein serine pyrophosphorylase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 523 |
| Chain | Residue |
| B | ARG9 |
| B | ASN41 |
| B | PHE42 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 524 |
| Chain | Residue |
| B | ARG422 |
| B | HIS423 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL B 525 |
| Chain | Residue |
| B | LYS180 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 526 |
| Chain | Residue |
| B | GLU502 |
| B | HOH552 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 523 |
| Chain | Residue |
| A | PHE42 |
| A | ARG9 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO B 527 |
| Chain | Residue |
| B | LYS390 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 528 |
| Chain | Residue |
| B | LEU77 |
| B | ASP83 |
| B | LYS271 |
| B | HOH584 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 30 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q16222 |
| Chain | Residue | Details |
| A | LEU108 | |
| A | GLU303 | |
| A | TYR304 | |
| A | ASN327 | |
| A | PHE381 | |
| A | LYS407 | |
| A | LYS472 | |
| B | LEU108 | |
| B | GLY110 | |
| B | GLY111 | |
| B | GLN196 | |
| A | GLY110 | |
| B | GLY222 | |
| B | ASN223 | |
| B | CYS251 | |
| B | VAL252 | |
| B | GLY290 | |
| B | GLU303 | |
| B | TYR304 | |
| B | ASN327 | |
| B | PHE381 | |
| B | LYS407 | |
| A | GLY111 | |
| B | LYS472 | |
| A | GLN196 | |
| A | GLY222 | |
| A | ASN223 | |
| A | CYS251 | |
| A | VAL252 | |
| A | GLY290 |
