Research workbench
Crystal structure of ATDHDPS1 in complex with mbdta-2
Analyse Crystal structure of ATDHDPS1 in complex with mbdta-2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MDS
- Type
- protein
- Length
- 618 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9LZX6
- Ligands
- YXP, CL
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 307 | — | Q9LZX6 |
| B | — | protein | 311 | — | Q9LZX6 |
Ligands and binding sites
- YXP · {(5Z)-5-[(4-methoxyphenyl)methylidene]-2,4-dioxo-1,3-thiazolidin-3-yl}acetic acid · ligand · 4 copies · chains A, B
- CL · Chloride ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7MDS · Crystal structure of AtDHDPS1 in complex with MBDTA-2 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9LZX6 · AlphaFold monomer V2.0 prediction for 4-hydroxy- tetrahydrodipicolinate synthase 1… · a predicted model of the same protein · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9LZX6
- Elsewhere: RCSB PDB 7MDS · PDBe 7MDS · UniProt Q9LZX6
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