5U4H
1.05 Angstrom Resolution Crystal Structure of UDP-N-acetylglucosamine 1-carboxyvinyltransferase from Acinetobacter baumannii in Covalently Bound Complex with (2R)-2-(phosphonooxy)propanoic Acid.
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | binding site for residue NA A 501 |
Chain | Residue |
A | GLU330 |
A | HOH801 |
A | HOH852 |
A | HOH1073 |
B | GLU330 |
B | HOH837 |
B | HOH841 |
B | HOH1080 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue NA A 502 |
Chain | Residue |
A | ASN23 |
A | HOH781 |
A | HOH833 |
A | HOH1033 |
A | HOH1042 |
A | LYS22 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue NA A 503 |
Chain | Residue |
A | ASP124 |
A | HOH954 |
B | ILE346 |
B | HOH711 |
B | HOH824 |
B | HOH895 |
B | HOH1144 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue NA A 504 |
Chain | Residue |
A | LYS89 |
A | HOH623 |
A | HOH644 |
A | HOH837 |
A | HOH932 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue NA A 505 |
Chain | Residue |
A | VAL139 |
A | HOH609 |
A | HOH665 |
A | HOH820 |
A | HOH868 |
A | HOH1180 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue NA A 506 |
Chain | Residue |
A | HOH647 |
A | HOH1015 |
A | HOH1192 |
A | HOH1199 |
B | HOH724 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue FMT A 507 |
Chain | Residue |
A | LYS22 |
A | ASN23 |
A | ASP306 |
A | ARG332 |
A | ARG372 |
site_id | AC8 |
Number of Residues | 11 |
Details | binding site for residue FMT A 508 |
Chain | Residue |
A | ASN23 |
A | VAL164 |
A | GLU189 |
A | GLU191 |
A | ARG233 |
A | HOH625 |
A | HOH640 |
A | HOH768 |
A | HOH781 |
A | HOH833 |
A | HOH835 |
site_id | AC9 |
Number of Residues | 15 |
Details | binding site for residue 0V5 A 509 |
Chain | Residue |
A | MET91 |
A | ARG92 |
A | CYS116 |
A | ILE118 |
A | ARG398 |
A | HOH623 |
A | HOH644 |
A | HOH646 |
A | HOH654 |
A | HOH666 |
A | HOH685 |
A | HOH695 |
A | HOH707 |
A | HOH788 |
A | HOH924 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue NA B 501 |
Chain | Residue |
B | LYS22 |
B | ASN23 |
B | HOH772 |
B | HOH828 |
B | HOH1026 |
B | HOH1034 |
site_id | AD2 |
Number of Residues | 7 |
Details | binding site for residue NA B 502 |
Chain | Residue |
A | ILE346 |
A | HOH723 |
A | HOH810 |
A | HOH842 |
A | HOH1147 |
B | ASP124 |
B | HOH934 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue NA B 503 |
Chain | Residue |
B | VAL139 |
B | HOH667 |
B | HOH756 |
B | HOH848 |
B | HOH1025 |
B | HOH1152 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue FMT B 504 |
Chain | Residue |
B | LYS22 |
B | ASN23 |
B | ASP306 |
B | ARG332 |
B | ARG372 |
site_id | AD5 |
Number of Residues | 11 |
Details | binding site for residue FMT B 505 |
Chain | Residue |
B | HOH728 |
B | HOH772 |
B | HOH817 |
B | HOH828 |
B | ASN23 |
B | VAL164 |
B | GLU189 |
B | GLU191 |
B | ARG233 |
B | HOH625 |
B | HOH648 |
site_id | AD6 |
Number of Residues | 19 |
Details | binding site for Di-peptide 0V5 B 506 and CYS B 116 |
Chain | Residue |
B | MET91 |
B | ARG92 |
B | GLY115 |
B | ALA117 |
B | ILE118 |
B | GLY119 |
B | SER120 |
B | ARG398 |
B | HOH614 |
B | HOH641 |
B | HOH645 |
B | HOH654 |
B | HOH671 |
B | HOH689 |
B | HOH701 |
B | HOH721 |
B | HOH815 |
B | HOH916 |
B | HOH920 |