1YL7
the crystal structure of Mycobacterium tuberculosis dihydrodipicolinate reductase (Rv2773c) in complex with NADH (crystal form C)
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 activity |
| A | 0009085 | biological_process | L-lysine biosynthetic process |
| A | 0009089 | biological_process | obsolete L-lysine biosynthetic process via diaminopimelate |
| A | 0016726 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor |
| A | 0019877 | biological_process | obsolete 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 activity |
| B | 0009085 | biological_process | L-lysine biosynthetic process |
| B | 0009089 | biological_process | obsolete L-lysine biosynthetic process via diaminopimelate |
| B | 0016726 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor |
| B | 0019877 | biological_process | obsolete 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 |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase activity |
| C | 0009085 | biological_process | L-lysine biosynthetic process |
| C | 0009089 | biological_process | obsolete L-lysine biosynthetic process via diaminopimelate |
| C | 0016726 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor |
| C | 0019877 | biological_process | obsolete diaminopimelate biosynthetic process |
| C | 0050661 | molecular_function | NADP binding |
| C | 0051287 | molecular_function | NAD binding |
| C | 0070402 | molecular_function | NADPH binding |
| C | 0070404 | molecular_function | NADH binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase activity |
| D | 0009085 | biological_process | L-lysine biosynthetic process |
| D | 0009089 | biological_process | obsolete L-lysine biosynthetic process via diaminopimelate |
| D | 0016726 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor |
| D | 0019877 | biological_process | obsolete diaminopimelate biosynthetic process |
| D | 0050661 | molecular_function | NADP binding |
| D | 0051287 | molecular_function | NAD binding |
| D | 0070402 | molecular_function | NADPH binding |
| D | 0070404 | molecular_function | NADH binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0005829 | cellular_component | cytosol |
| E | 0005886 | cellular_component | plasma membrane |
| E | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase activity |
| E | 0009085 | biological_process | L-lysine biosynthetic process |
| E | 0009089 | biological_process | obsolete L-lysine biosynthetic process via diaminopimelate |
| E | 0016726 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor |
| E | 0019877 | biological_process | obsolete diaminopimelate biosynthetic process |
| E | 0050661 | molecular_function | NADP binding |
| E | 0051287 | molecular_function | NAD binding |
| E | 0070402 | molecular_function | NADPH binding |
| E | 0070404 | molecular_function | NADH binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0005829 | cellular_component | cytosol |
| F | 0005886 | cellular_component | plasma membrane |
| F | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase activity |
| F | 0009085 | biological_process | L-lysine biosynthetic process |
| F | 0009089 | biological_process | obsolete L-lysine biosynthetic process via diaminopimelate |
| F | 0016726 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor |
| F | 0019877 | biological_process | obsolete diaminopimelate biosynthetic process |
| F | 0050661 | molecular_function | NADP binding |
| F | 0051287 | molecular_function | NAD binding |
| F | 0070402 | molecular_function | NADPH binding |
| F | 0070404 | molecular_function | NADH binding |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0005829 | cellular_component | cytosol |
| G | 0005886 | cellular_component | plasma membrane |
| G | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase activity |
| G | 0009085 | biological_process | L-lysine biosynthetic process |
| G | 0009089 | biological_process | obsolete L-lysine biosynthetic process via diaminopimelate |
| G | 0016726 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor |
| G | 0019877 | biological_process | obsolete diaminopimelate biosynthetic process |
| G | 0050661 | molecular_function | NADP binding |
| G | 0051287 | molecular_function | NAD binding |
| G | 0070402 | molecular_function | NADPH binding |
| G | 0070404 | molecular_function | NADH binding |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0005829 | cellular_component | cytosol |
| H | 0005886 | cellular_component | plasma membrane |
| H | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase activity |
| H | 0009085 | biological_process | L-lysine biosynthetic process |
| H | 0009089 | biological_process | obsolete L-lysine biosynthetic process via diaminopimelate |
| H | 0016726 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor |
| H | 0019877 | biological_process | obsolete diaminopimelate biosynthetic process |
| H | 0050661 | molecular_function | NADP binding |
| H | 0051287 | molecular_function | NAD binding |
| H | 0070402 | molecular_function | NADPH binding |
| H | 0070404 | molecular_function | NADH binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 401 |
| Chain | Residue |
| D | VAL20 |
| D | ALA21 |
| D | ALA23 |
| D | LEU26 |
| D | HOH505 |
| D | HOH585 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG G 402 |
| Chain | Residue |
| G | LEU26 |
| G | HOH511 |
| G | VAL20 |
| G | ALA21 |
| G | ALA23 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG E 403 |
| Chain | Residue |
| E | VAL20 |
| E | ALA21 |
| E | ALA23 |
| E | LEU26 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 404 |
| Chain | Residue |
| B | VAL20 |
| B | ALA21 |
| B | ALA23 |
| B | LEU26 |
| B | HOH555 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 405 |
| Chain | Residue |
| A | VAL20 |
| A | ALA21 |
| A | ALA23 |
| A | LEU26 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG F 406 |
| Chain | Residue |
| F | VAL20 |
| F | ALA21 |
| F | ALA23 |
| F | LEU26 |
| site_id | AC7 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE NAI A 501 |
| Chain | Residue |
| A | GLY7 |
| A | LYS9 |
| A | GLY10 |
| A | LYS11 |
| A | VAL12 |
| A | LEU32 |
| A | ASP33 |
| A | ALA34 |
| A | PHE52 |
| A | THR53 |
| A | VAL57 |
| A | GLY75 |
| A | THR76 |
| A | THR77 |
| A | ALA102 |
| A | PRO103 |
| A | ASN104 |
| A | PHE105 |
| A | PHE217 |
| A | HOH503 |
| A | HOH512 |
| site_id | AC8 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE NAI B 502 |
| Chain | Residue |
| B | GLY7 |
| B | LYS9 |
| B | GLY10 |
| B | LYS11 |
| B | VAL12 |
| B | LEU32 |
| 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 | PHE217 |
| B | HOH516 |
| site_id | AC9 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NAI C 503 |
| Chain | Residue |
| C | GLY7 |
| C | LYS9 |
| C | GLY10 |
| C | LYS11 |
| C | VAL12 |
| C | ASP33 |
| C | ALA34 |
| C | PHE52 |
| C | THR53 |
| C | VAL57 |
| C | GLY75 |
| C | THR77 |
| C | ALA102 |
| C | PRO103 |
| C | ASN104 |
| C | PHE105 |
| C | PHE217 |
| C | HOH529 |
| site_id | BC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAI D 504 |
| Chain | Residue |
| D | VAL57 |
| D | GLY75 |
| D | THR77 |
| D | ALA102 |
| D | PRO103 |
| D | ASN104 |
| D | PHE105 |
| D | PHE217 |
| D | HOH510 |
| D | HOH511 |
| D | HOH524 |
| D | HOH527 |
| D | HOH546 |
| D | HOH580 |
| C | SER166 |
| C | THR167 |
| C | HOH505 |
| D | GLY7 |
| D | LYS9 |
| D | GLY10 |
| D | LYS11 |
| D | VAL12 |
| D | ASP33 |
| D | ALA34 |
| D | PHE52 |
| D | THR53 |
| site_id | BC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NAI E 505 |
| Chain | Residue |
| E | GLY7 |
| E | LYS9 |
| E | GLY10 |
| E | LYS11 |
| E | VAL12 |
| E | ASP33 |
| E | ALA34 |
| E | PHE52 |
| E | THR53 |
| E | VAL57 |
| E | GLY75 |
| E | THR76 |
| E | THR77 |
| E | ALA102 |
| E | PRO103 |
| E | ASN104 |
| E | PHE105 |
| E | PHE217 |
| E | HOH507 |
| site_id | BC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NAI F 506 |
| Chain | Residue |
| F | LEU6 |
| F | GLY7 |
| F | GLY10 |
| F | LYS11 |
| F | VAL12 |
| F | ASP33 |
| F | ALA34 |
| F | PHE52 |
| F | THR53 |
| F | VAL57 |
| F | GLY75 |
| F | THR76 |
| F | THR77 |
| F | ALA102 |
| F | PRO103 |
| F | ASN104 |
| F | PHE105 |
| F | HOH513 |
| site_id | BC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAI G 507 |
| Chain | Residue |
| G | LEU6 |
| G | GLY7 |
| G | LYS9 |
| G | GLY10 |
| G | LYS11 |
| G | VAL12 |
| G | LEU32 |
| G | ASP33 |
| G | ALA34 |
| G | PHE52 |
| G | THR53 |
| G | GLY75 |
| G | THR76 |
| G | THR77 |
| G | ALA102 |
| G | PRO103 |
| G | ASN104 |
| G | PHE105 |
| G | PHE217 |
| G | HOH508 |
| G | HOH524 |
| G | HOH563 |
| site_id | BC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NAI H 508 |
| Chain | Residue |
| H | GLY7 |
| H | LYS9 |
| H | GLY10 |
| H | LYS11 |
| H | VAL12 |
| H | ASP33 |
| H | ALA34 |
| H | PHE52 |
| H | THR53 |
| H | VAL57 |
| H | GLY75 |
| H | THR77 |
| H | ALA102 |
| H | PRO103 |
| H | ASN104 |
| H | PHE105 |
| H | PHE217 |
| H | HOH515 |
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 | 8 |
| 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 | 8 |
| Details | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 56 |
| 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 | 8 |
| 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 | 16 |
| 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 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1arz |
| Chain | Residue | Details |
| C | LYS136 | |
| C | HIS132 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1arz |
| Chain | Residue | Details |
| D | LYS136 | |
| D | HIS132 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1arz |
| Chain | Residue | Details |
| E | LYS136 | |
| E | HIS132 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1arz |
| Chain | Residue | Details |
| F | LYS136 | |
| F | HIS132 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1arz |
| Chain | Residue | Details |
| G | LYS136 | |
| G | HIS132 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1arz |
| Chain | Residue | Details |
| H | LYS136 | |
| H | HIS132 |






