1P9L
Structure of M. tuberculosis dihydrodipicolinate reductase in complex with NADH and 2,6 PDC
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase |
| A | 0009085 | biological_process | lysine biosynthetic process |
| A | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| A | 0009274 | cellular_component | peptidoglycan-based cell wall |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016726 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor |
| A | 0019877 | biological_process | diaminopimelate biosynthetic process |
| A | 0050661 | molecular_function | NADP binding |
| A | 0051287 | molecular_function | NAD binding |
| A | 0070402 | molecular_function | NADPH binding |
| A | 0070404 | molecular_function | NADH binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase |
| B | 0009085 | biological_process | lysine biosynthetic process |
| B | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| B | 0009274 | cellular_component | peptidoglycan-based cell wall |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016726 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor |
| B | 0019877 | biological_process | diaminopimelate biosynthetic process |
| B | 0050661 | molecular_function | NADP binding |
| B | 0051287 | molecular_function | NAD binding |
| B | 0070402 | molecular_function | NADPH binding |
| B | 0070404 | molecular_function | NADH binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAI A 301 |
| Chain | Residue |
| A | GLY7 |
| A | VAL57 |
| A | GLY75 |
| A | THR77 |
| A | ALA102 |
| A | PRO103 |
| A | ASN104 |
| A | PHE105 |
| A | LYS136 |
| A | PHE217 |
| A | PDC302 |
| A | LYS9 |
| A | HOH916 |
| A | HOH927 |
| A | HOH935 |
| A | GLY10 |
| A | LYS11 |
| A | VAL12 |
| A | ASP33 |
| A | ALA34 |
| A | PHE52 |
| A | THR53 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PDC A 302 |
| Chain | Residue |
| A | THR77 |
| A | PRO103 |
| A | ASN104 |
| A | HIS133 |
| A | LYS136 |
| A | SER141 |
| A | GLY142 |
| A | THR143 |
| A | NAI301 |
| A | HOH916 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAI B 401 |
| Chain | Residue |
| B | LEU6 |
| B | GLY7 |
| B | LYS9 |
| B | GLY10 |
| B | LYS11 |
| B | VAL12 |
| B | ASP33 |
| B | ALA34 |
| B | PHE52 |
| B | THR53 |
| B | VAL57 |
| B | GLY75 |
| B | THR76 |
| B | THR77 |
| B | ALA102 |
| B | PRO103 |
| B | ASN104 |
| B | PHE105 |
| B | LYS136 |
| B | PHE217 |
| B | PDC402 |
| B | HOH1401 |
| B | HOH1420 |
| B | HOH1428 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PDC B 402 |
| Chain | Residue |
| B | THR77 |
| B | PRO103 |
| B | ASN104 |
| B | HIS133 |
| B | LYS136 |
| B | ASP138 |
| B | SER141 |
| B | GLY142 |
| B | THR143 |
| B | NAI401 |
| B | HOH1420 |
| B | HOH1428 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PG4 B 2000 |
| Chain | Residue |
| A | THR206 |
| A | ARG208 |
| A | ASP210 |
| B | LEU190 |
| B | ARG208 |
| B | ASP210 |
Functional Information from PROSITE/UniProt
| site_id | PS01298 |
| Number of Residues | 18 |
| Details | DAPB Dihydrodipicolinate reductase signature. EViElHhphKaDapSGTA |
| Chain | Residue | Details |
| A | GLU127-ALA144 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00102","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12962488","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1C3V","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12962488","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20057050","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1P9L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YL7","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12962488","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1C3V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1P9L","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1arz |
| Chain | Residue | Details |
| A | LYS136 | |
| A | HIS132 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1arz |
| Chain | Residue | Details |
| B | LYS136 | |
| B | HIS132 |
