4DPQ
The structure of dihydrodipicolinate synthase 2 from Arabidopsis thaliana in complex with (S)-lysine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0008840 | molecular_function | 4-hydroxy-tetrahydrodipicolinate synthase activity |
| A | 0009085 | biological_process | lysine biosynthetic process |
| A | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| A | 0009507 | cellular_component | chloroplast |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019877 | biological_process | diaminopimelate biosynthetic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0008840 | molecular_function | 4-hydroxy-tetrahydrodipicolinate synthase activity |
| B | 0009085 | biological_process | lysine biosynthetic process |
| B | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| B | 0009507 | cellular_component | chloroplast |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019877 | biological_process | diaminopimelate biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE NA A 401 |
| Chain | Residue |
| A | PHE345 |
| A | VAL346 |
| A | GLY347 |
| A | NA402 |
| A | HOH542 |
| A | HOH545 |
| A | HOH553 |
| A | HOH588 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 402 |
| Chain | Residue |
| A | NA401 |
| A | HOH542 |
| A | HOH553 |
| A | HOH588 |
| A | HOH647 |
| A | GLU343 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 403 |
| Chain | Residue |
| A | ARG252 |
| A | HOH525 |
| A | HOH532 |
| A | HOH543 |
| A | HOH565 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE LYS A 404 |
| Chain | Residue |
| A | GLY111 |
| A | GLN112 |
| A | MET114 |
| A | TRP116 |
| A | HIS119 |
| A | TYR169 |
| A | HOH509 |
| A | HOH548 |
| B | ASN143 |
| B | GLU147 |
| B | LYS403 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE NA B 401 |
| Chain | Residue |
| B | PHE345 |
| B | VAL346 |
| B | GLY347 |
| B | NA402 |
| B | HOH520 |
| B | HOH556 |
| B | HOH557 |
| B | HOH617 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 402 |
| Chain | Residue |
| B | GLU343 |
| B | NA401 |
| B | HOH520 |
| B | HOH556 |
| B | HOH617 |
| B | HOH629 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE LYS B 403 |
| Chain | Residue |
| A | ASN143 |
| A | GLU147 |
| A | LYS404 |
| B | GLY111 |
| B | GLN112 |
| B | MET114 |
| B | TRP116 |
| B | HIS119 |
| B | TYR169 |
| B | HOH515 |
| B | HOH528 |
| B | HOH588 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Schiff-base intermediate with substrate","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Site: {"description":"Part of a proton relay during catalysis","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
