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 | 0009089 | biological_process | obsolete L-lysine biosynthetic process via diaminopimelate |
| A | 0016829 | molecular_function | lyase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008840 | molecular_function | 4-hydroxy-tetrahydrodipicolinate synthase activity |
| B | 0009089 | biological_process | obsolete L-lysine biosynthetic process via diaminopimelate |
| B | 0016829 | molecular_function | lyase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0008840 | molecular_function | 4-hydroxy-tetrahydrodipicolinate synthase activity |
| C | 0009089 | biological_process | obsolete L-lysine biosynthetic process via diaminopimelate |
| C | 0016829 | molecular_function | lyase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0008840 | molecular_function | 4-hydroxy-tetrahydrodipicolinate synthase activity |
| D | 0009089 | biological_process | obsolete L-lysine biosynthetic process via diaminopimelate |
| D | 0016829 | molecular_function | lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 301 |
| Chain | Residue |
| B | ARG138 |
| B | PHE245 |
| B | GLU247 |
| B | PRO248 |
| B | GLY249 |
| B | HOH542 |
| B | HOH563 |
| B | HOH653 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 302 |
| Chain | Residue |
| B | PRO137 |
| B | HOH448 |
| B | HOH484 |
| B | HOH592 |
| B | HOH718 |
| B | PRO136 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 303 |
| Chain | Residue |
| B | LYS57 |
| B | LEU90 |
| B | HIS91 |
| B | ASP94 |
| B | HOH501 |
| B | HOH582 |
| B | HOH696 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 304 |
| Chain | Residue |
| B | GLU21 |
| B | ASP54 |
| B | ARG58 |
| B | HOH541 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL C 301 |
| Chain | Residue |
| C | THR111 |
| C | GLN112 |
| C | HOH467 |
| C | HOH507 |
| C | HOH662 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL D 301 |
| Chain | Residue |
| D | TYR133 |
| D | ILE135 |
| D | ARG138 |
| D | LYS162 |
| D | GLY187 |
| D | PHE245 |
| D | GOL302 |
| D | HOH429 |
| D | HOH484 |
| D | HOH513 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D 302 |
| Chain | Residue |
| C | HOH621 |
| D | ARG138 |
| D | PHE245 |
| D | PRO248 |
| D | GLY249 |
| D | GOL301 |
| D | HOH590 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL D 303 |
| Chain | Residue |
| B | ALA25 |
| B | ALA26 |
| B | GLU29 |
| B | HOH523 |
| B | HOH754 |
| D | ASP284 |
| D | HOH451 |
| D | HOH467 |
| D | HOH505 |
Functional Information from PROSITE/UniProt
| site_id | PS00665 |
| Number of Residues | 18 |
| Details | DHDPS_1 Dihydrodipicolinate synthase signature 1. GLVpvGTTGESptlshdE |
| Chain | Residue | Details |
| A | GLY38-GLU55 | |
| site_id | PS00666 |
| Number of Residues | 32 |
| Details | DHDPS_2 Dihydrodipicolinate synthase signature 2. YNIPprSvvdMspetmgalvkahknIvGVKDA |
| Chain | Residue | Details |
| A | TYR133-ALA164 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00418","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Schiff-base intermediate with substrate","evidences":[{"source":"HAMAP-Rule","id":"MF_00418","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24677246","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00418","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24677246","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00418","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Site: {"description":"Part of a proton relay during catalysis","evidences":[{"source":"HAMAP-Rule","id":"MF_00418","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Site: {"description":"L-lysine inhibitor binding; via carbonyl oxygen","evidences":[{"source":"PubMed","id":"24677246","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 16 |
| Details | Site: {"description":"L-lysine inhibitor binding","evidences":[{"source":"PubMed","id":"24677246","evidenceCode":"ECO:0000269"}]} |
4I7U
