5BQ2
Crystal structure of UDP-N-acetylglucosamine 1-carboxyvinyltransferase (UDP-N-acetylglucosamine enolpyruvyl transferase, EPT) from Pseudomonas aeruginosa
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0008760 | molecular_function | UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| A | 0019277 | biological_process | UDP-N-acetylgalactosamine biosynthetic process |
| A | 0051301 | biological_process | cell division |
| A | 0071555 | biological_process | cell wall organization |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008360 | biological_process | regulation of cell shape |
| B | 0008760 | molecular_function | UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| B | 0019277 | biological_process | UDP-N-acetylgalactosamine biosynthetic process |
| B | 0051301 | biological_process | cell division |
| B | 0071555 | biological_process | cell wall organization |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008360 | biological_process | regulation of cell shape |
| C | 0008760 | molecular_function | UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity |
| C | 0009252 | biological_process | peptidoglycan biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| C | 0019277 | biological_process | UDP-N-acetylgalactosamine biosynthetic process |
| C | 0051301 | biological_process | cell division |
| C | 0071555 | biological_process | cell wall organization |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0008360 | biological_process | regulation of cell shape |
| D | 0008760 | molecular_function | UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity |
| D | 0009252 | biological_process | peptidoglycan biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| D | 0019277 | biological_process | UDP-N-acetylgalactosamine biosynthetic process |
| D | 0051301 | biological_process | cell division |
| D | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 33 |
| Details | binding site for residue EPU A 501 |
| Chain | Residue |
| A | LYS22 |
| A | VAL164 |
| A | SER165 |
| A | VAL166 |
| A | THR167 |
| A | ASP308 |
| A | VAL330 |
| A | PHE331 |
| A | LEU373 |
| A | HOH631 |
| A | HOH642 |
| A | ASN23 |
| A | HOH648 |
| A | HOH657 |
| A | HOH664 |
| A | HOH668 |
| A | HOH673 |
| A | HOH677 |
| A | HOH785 |
| A | HOH801 |
| A | HOH820 |
| A | HOH834 |
| A | SER121 |
| A | HOH854 |
| A | HOH857 |
| A | HOH870 |
| A | HOH893 |
| A | ARG122 |
| A | PRO123 |
| A | VAL124 |
| A | ASP125 |
| A | LEU126 |
| A | THR163 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 502 |
| Chain | Residue |
| A | QPA117 |
| A | HOH684 |
| A | HOH698 |
| A | HOH903 |
| A | HOH938 |
| site_id | AC3 |
| Number of Residues | 30 |
| Details | binding site for residue EPU B 501 |
| Chain | Residue |
| B | LYS22 |
| B | ASN23 |
| B | SER121 |
| B | ARG122 |
| B | PRO123 |
| B | VAL124 |
| B | ASP125 |
| B | LEU126 |
| B | THR163 |
| B | VAL164 |
| B | SER165 |
| B | VAL166 |
| B | THR167 |
| B | ASP308 |
| B | VAL330 |
| B | PHE331 |
| B | LEU373 |
| B | HOH641 |
| B | HOH665 |
| B | HOH671 |
| B | HOH684 |
| B | HOH687 |
| B | HOH721 |
| B | HOH742 |
| B | HOH802 |
| B | HOH812 |
| B | HOH836 |
| B | HOH874 |
| B | HOH894 |
| B | HOH917 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 502 |
| Chain | Residue |
| B | QPA117 |
| B | HOH639 |
| B | HOH680 |
| B | HOH868 |
| B | HOH925 |
| site_id | AC5 |
| Number of Residues | 32 |
| Details | binding site for residue EPU C 501 |
| Chain | Residue |
| C | HOH821 |
| C | HOH839 |
| C | HOH844 |
| C | HOH860 |
| C | HOH928 |
| C | HOH931 |
| C | LYS22 |
| C | ASN23 |
| C | SER121 |
| C | ARG122 |
| C | PRO123 |
| C | VAL124 |
| C | ASP125 |
| C | LEU126 |
| C | THR163 |
| C | VAL164 |
| C | SER165 |
| C | VAL166 |
| C | THR167 |
| C | ASP308 |
| C | VAL330 |
| C | PHE331 |
| C | LEU373 |
| C | HOH636 |
| C | HOH673 |
| C | HOH680 |
| C | HOH682 |
| C | HOH696 |
| C | HOH704 |
| C | HOH715 |
| C | HOH773 |
| C | HOH818 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 502 |
| Chain | Residue |
| C | QPA117 |
| C | HOH675 |
| C | HOH732 |
| C | HOH900 |
| C | HOH918 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue MG C 503 |
| Chain | Residue |
| A | HOH876 |
| B | HOH688 |
| B | HOH736 |
| C | ASN353 |
| C | HOH764 |
| C | HOH921 |
| site_id | AC8 |
| Number of Residues | 33 |
| Details | binding site for residue EPU D 501 |
| Chain | Residue |
| D | LYS22 |
| D | ASN23 |
| D | ALA94 |
| D | SER121 |
| D | ARG122 |
| D | PRO123 |
| D | VAL124 |
| D | ASP125 |
| D | LEU126 |
| D | THR163 |
| D | VAL164 |
| D | SER165 |
| D | VAL166 |
| D | THR167 |
| D | ASP308 |
| D | VAL330 |
| D | PHE331 |
| D | LEU373 |
| D | HOH656 |
| D | HOH673 |
| D | HOH674 |
| D | HOH681 |
| D | HOH683 |
| D | HOH687 |
| D | HOH693 |
| D | HOH700 |
| D | HOH706 |
| D | HOH751 |
| D | HOH796 |
| D | HOH864 |
| D | HOH876 |
| D | HOH893 |
| D | HOH952 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue MG D 502 |
| Chain | Residue |
| D | QPA117 |
| D | HOH646 |
| D | HOH670 |
| D | HOH902 |
| D | HOH933 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue MG D 503 |
| Chain | Residue |
| A | HOH622 |
| A | HOH670 |
| B | HOH851 |
| D | ASN353 |
| D | HOH806 |
| D | HOH926 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00111 |
| Chain | Residue | Details |
| A | QPA117 | |
| B | QPA117 | |
| C | QPA117 | |
| D | QPA117 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0007744|PDB:5BQ2 |
| Chain | Residue | Details |
| A | LYS22 | |
| B | VAL330 | |
| C | LYS22 | |
| C | ARG122 | |
| C | SER165 | |
| C | ASP308 | |
| C | VAL330 | |
| D | LYS22 | |
| D | ARG122 | |
| D | SER165 | |
| D | ASP308 | |
| A | ARG122 | |
| D | VAL330 | |
| A | SER165 | |
| A | ASP308 | |
| A | VAL330 | |
| B | LYS22 | |
| B | ARG122 | |
| B | SER165 | |
| B | ASP308 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00111 |
| Chain | Residue | Details |
| A | ARG93 | |
| B | ARG93 | |
| C | ARG93 | |
| D | ARG93 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: 2-(S-cysteinyl)pyruvic acid O-phosphothioketal => ECO:0000255|HAMAP-Rule:MF_00111 |
| Chain | Residue | Details |
| A | QPA117 | |
| B | QPA117 | |
| C | QPA117 | |
| D | QPA117 |
