5T26
Kinetic, Spectral and Structural Characterization of the Slow Binding Inhibitor Acetopyruvate with Dihydrodipicolinate Synthase from Escherichia coli.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008840 | molecular_function | 4-hydroxy-tetrahydrodipicolinate synthase activity |
| A | 0009085 | biological_process | lysine biosynthetic process |
| A | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019877 | biological_process | diaminopimelate biosynthetic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0044281 | biological_process | small molecule metabolic process |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008840 | molecular_function | 4-hydroxy-tetrahydrodipicolinate synthase activity |
| B | 0009085 | biological_process | lysine biosynthetic process |
| B | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019877 | biological_process | diaminopimelate biosynthetic process |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0044281 | biological_process | small molecule metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 301 |
| Chain | Residue |
| A | LEU243 |
| A | ASN248 |
| A | PRO249 |
| A | PRO251 |
| A | VAL252 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 302 |
| Chain | Residue |
| A | GLU47 |
| A | LYS253 |
| A | VAL10 |
| A | THR11 |
| A | THR45 |
| A | GLY46 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue NA A 303 |
| Chain | Residue |
| A | SER5 |
| A | THR36 |
| A | ALA211 |
| A | ALA215 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 304 |
| Chain | Residue |
| A | PRO105 |
| A | TYR106 |
| A | TYR107 |
| A | ARG109 |
| A | THR139 |
| A | CYS141 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 305 |
| Chain | Residue |
| A | SER185 |
| A | ASP187 |
| A | SER190 |
| A | PHE194 |
| A | HOH471 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 301 |
| Chain | Residue |
| B | VAL10 |
| B | THR11 |
| B | THR45 |
| B | GLY46 |
| B | GLU47 |
| B | LYS253 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue NA B 302 |
| Chain | Residue |
| B | LEU243 |
| B | ASN248 |
| B | PRO249 |
| B | PRO251 |
| B | VAL252 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | binding site for residue TLA B 303 |
| Chain | Residue |
| A | VAL231 |
| A | ARG235 |
| B | GLY224 |
| B | HIS225 |
| B | PHE226 |
| B | ALA227 |
| B | GLU228 |
| B | HOH416 |
| B | HOH441 |
| B | HOH448 |
| B | HOH517 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 304 |
| Chain | Residue |
| B | SER48 |
| B | ALA49 |
| B | ASN80 |
| B | TYR106 |
| B | TYR107 |
Functional Information from PROSITE/UniProt
| site_id | PS00665 |
| Number of Residues | 18 |
| Details | DHDPS_1 Dihydrodipicolinate synthase signature 1. AIVsvGTTGESatlnhdE |
| Chain | Residue | Details |
| A | ALA38-GLU55 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor |
| Chain | Residue | Details |
| A | TYR133 | |
| B | TYR133 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Schiff-base intermediate with substrate |
| Chain | Residue | Details |
| A | 74P161 | |
| B | 74P161 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00418, ECO:0000269|PubMed:20353808, ECO:0000269|PubMed:22552955 |
| Chain | Residue | Details |
| B | THR45 | |
| B | ILE203 | |
| A | THR45 | |
| A | ILE203 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | SITE: Part of a proton relay during catalysis |
| Chain | Residue | Details |
| B | THR44 | |
| B | TYR107 | |
| A | THR44 | |
| A | TYR107 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | SITE: L-lysine inhibitor binding; via carbonyl oxygen |
| Chain | Residue | Details |
| A | ALA49 | |
| B | ALA49 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | SITE: L-lysine inhibitor binding |
| Chain | Residue | Details |
| A | TYR106 | |
| B | ASN80 | |
| B | GLU84 | |
| B | TYR106 | |
| A | ASN80 | |
| A | GLU84 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 267 |
| Chain | Residue | Details |
| A | ARG138 | electrostatic stabiliser |
| A | 74P161 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | ILE203 | activator, increase electrophilicity, polar interaction, steric role |
| A | THR44 | hydrogen bond acceptor, hydrogen bond donor |
| A | TYR107 | hydrogen bond donor |
| A | TYR133 | activator, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 267 |
| Chain | Residue | Details |
| B | THR44 | hydrogen bond acceptor, hydrogen bond donor |
| B | TYR107 | hydrogen bond donor |
| B | TYR133 | activator, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | ARG138 | electrostatic stabiliser |
| B | 74P161 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | ILE203 | activator, increase electrophilicity, polar interaction, steric role |
