MolNFT v1 · #4621 · protein
Mandelate racemase mutant D270N co-crystallized with (S)-atrolactate
1DTN: “Mandelate racemase mutant D270N co-crystallized with (S)-atrolactate”. X-ray diffraction, 2 ligands (APG, MG), 1 pocket (best druggability 0.64). MolNFT v1 #4621 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1DTN
- Type
- protein
- Length
- 357 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mandelate racemase
- EC
- 5.1.2.2
- UniProt
- P11444
- Ligands
- APG, MG
- Pockets
- 1 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mandelate racemase (EC 5.1.2.2) | protein | 357 | 41% helix, 23% strand | P11444 |
Ligands and binding sites
- APG · Atrolactic acid (2-phenyl-lactic acid) · ligand · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 336 | 0.64 | 0.80 | 39 | APG |
Compared structures
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 P11444
- Elsewhere: RCSB PDB 1DTN · PDBe 1DTN · UniProt P11444
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