1C3V
DIHYDRODIPICOLINATE REDUCTASE FROM MYCOBACTERIUM TUBERCULOSIS COMPLEXED WITH NADPH AND 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 | 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 | 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 | 19 |
| Details | BINDING SITE FOR RESIDUE NDP A 801 |
| Chain | Residue |
| A | GLY507 |
| A | VAL557 |
| A | GLY575 |
| A | THR577 |
| A | ALA602 |
| A | PRO603 |
| A | ASN604 |
| A | PHE605 |
| A | LYS636 |
| A | PHE717 |
| A | PDC802 |
| A | LYS509 |
| A | GLY510 |
| A | LYS511 |
| A | VAL512 |
| A | ASP533 |
| A | ALA534 |
| A | PHE552 |
| A | THR553 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NDP B 1301 |
| Chain | Residue |
| B | GLY1007 |
| B | LYS1009 |
| B | GLY1010 |
| B | LYS1011 |
| B | VAL1012 |
| B | ASP1033 |
| B | ALA1034 |
| B | PHE1052 |
| B | THR1053 |
| B | VAL1057 |
| B | GLY1075 |
| B | THR1076 |
| B | THR1077 |
| B | ALA1102 |
| B | PRO1103 |
| B | ASN1104 |
| B | PHE1105 |
| B | LYS1136 |
| B | PHE1217 |
| B | PDC1302 |
| B | HOH2009 |
| B | HOH2016 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PDC A 802 |
| Chain | Residue |
| A | THR577 |
| A | PRO603 |
| A | ASN604 |
| A | HIS633 |
| A | LYS636 |
| A | SER641 |
| A | GLY642 |
| A | THR643 |
| A | ALA692 |
| A | NDP801 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PDC B 1302 |
| Chain | Residue |
| B | THR1077 |
| B | PRO1103 |
| B | ASN1104 |
| B | HIS1133 |
| B | LYS1136 |
| B | SER1141 |
| B | GLY1142 |
| B | THR1143 |
| B | ALA1192 |
| B | NDP1301 |
| B | HOH2009 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PG4 B 2000 |
| Chain | Residue |
| A | THR704 |
| A | THR706 |
| A | ARG708 |
| A | ASP710 |
| B | ARG1208 |
| B | ASP1210 |
Functional Information from PROSITE/UniProt
| site_id | PS01298 |
| Number of Residues | 18 |
| Details | DAPB Dihydrodipicolinate reductase signature. EViElHhphKaDapSGTA |
| Chain | Residue | Details |
| A | GLU627-ALA644 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00102 |
| Chain | Residue | Details |
| A | HIS632 | |
| B | HIS1132 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000305 |
| Chain | Residue | Details |
| A | LYS636 | |
| B | LYS1136 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12962488, ECO:0007744|PDB:1C3V |
| Chain | Residue | Details |
| A | LYS511 | |
| A | GLY575 | |
| A | ALA602 | |
| A | LYS636 | |
| B | LYS1011 | |
| B | GLY1075 | |
| B | ALA1102 | |
| B | LYS1136 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12962488, ECO:0000269|PubMed:20057050, ECO:0007744|PDB:1P9L, ECO:0007744|PDB:1YL7 |
| Chain | Residue | Details |
| A | ASP533 | |
| B | ASP1033 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:12962488, ECO:0007744|PDB:1C3V, ECO:0007744|PDB:1P9L |
| Chain | Residue | Details |
| A | HIS633 | |
| A | GLY642 | |
| B | HIS1133 | |
| B | GLY1142 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1arz |
| Chain | Residue | Details |
| A | HIS632 | |
| A | LYS636 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1arz |
| Chain | Residue | Details |
| B | HIS1132 | |
| B | LYS1136 |
