MolNFT v1 · #135373 · protein
Crystal structure of D-isomer specific 2-hydroxyacid dehydrogenase from desulfovibrio vulgaris
5TX7 · D-isomer specific 2-hydroxyacid dehydrogenase family protein: “Crystal structure of D-isomer specific 2-hydroxyacid dehydrogenase from desulfovibrio vulgaris”. X-ray diffraction, 2 pockets (best druggability 0.68). MolNFT v1 #135373…
- PDB
- 5TX7
- Type
- protein
- Length
- 645 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- D-isomer specific 2-hydroxyacid dehydrogenase family protein
- EC
- 1.1.1.-
- UniProt
- Q72C72
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | D-isomer specific 2-hydroxyacid dehydrogenase family protein (EC 1.1.1.-) | protein | 323 | 35% helix, 17% strand | Q72C72 |
| B | D-isomer specific 2-hydroxyacid dehydrogenase family protein (EC 1.1.1.-) | protein | 322 | 36% helix, 17% strand | Q72C72 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A, B
- PGE · Triethylene glycol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 574 | 0.68 | 0.78 | 65 | empty |
| 2 | 489 | 0.66 | 0.78 | 41 | empty |
Interfaces
1 interface between chains.
- A–B · 3021 Ų buried · 33 hydrogen bonds · protein-protein
Compared structures
- 5TX7 · Crystal structure of D-isomer specific 2-hydroxyacid dehydrogenase from Desulfovibrio… · the same entry in another collection · 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 Q72C72
- Elsewhere: RCSB PDB 5TX7 · PDBe 5TX7 · UniProt Q72C72
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