3IJP
Crystal structure of dihydrodipicolinate reductase from bartonella henselae at 2.0A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| 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 | 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 |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| 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 | 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 301 |
| Chain | Residue |
| A | ILE20 |
| A | ARG23 |
| A | VAL26 |
| A | HOH459 |
| A | HOH460 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 302 |
| Chain | Residue |
| A | HIS155 |
| A | LYS158 |
| A | HOH374 |
| site_id | AC3 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAP A 300 |
| Chain | Residue |
| A | ASN9 |
| A | GLY10 |
| A | ARG11 |
| A | MET12 |
| A | ARG34 |
| A | PHE74 |
| A | SER75 |
| A | GLN76 |
| A | TYR83 |
| A | GLY97 |
| A | THR99 |
| A | SER121 |
| A | GLY122 |
| A | ASN123 |
| A | MET124 |
| A | LYS158 |
| A | ASP160 |
| A | PHE238 |
| A | HOH280 |
| A | HOH282 |
| A | HOH306 |
| A | HOH314 |
| A | HOH349 |
| A | HOH379 |
| A | HOH393 |
| A | HOH397 |
| A | HOH425 |
| A | HOH444 |
| A | HOH454 |
| A | HOH474 |
| A | GLY7 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 301 |
| Chain | Residue |
| B | ILE20 |
| B | ARG23 |
| B | VAL26 |
| B | HOH332 |
| B | HOH481 |
| B | HOH494 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 302 |
| Chain | Residue |
| B | ALA8 |
| B | ASN9 |
| B | VAL33 |
| B | ARG34 |
| B | HOH416 |
Functional Information from PROSITE/UniProt
| site_id | PS01298 |
| Number of Residues | 18 |
| Details | DAPB Dihydrodipicolinate reductase signature. EIyEmHhanKvDspSGTA |
| Chain | Residue | Details |
| A | GLU149-ALA166 |
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":[{"source":"HAMAP-Rule","id":"MF_00102","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 26 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00102","evidenceCode":"ECO:0000255"}]} |
| 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 | HIS154 | |
| A | LYS158 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1arz |
| Chain | Residue | Details |
| B | HIS154 | |
| B | LYS158 |
