MolNFT v1 · #149469 · protein
Amine dehydrogenase from petrotoga mobilis; open form
6G1H · Dihydrodipicolinate reductase: “Amine dehydrogenase from petrotoga mobilis; open form”. X-ray diffraction, 1 ligand (NAD), 2 pockets (best druggability 0.66). MolNFT v1 #149469 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 6G1H
- Type
- protein
- Length
- 342 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydrodipicolinate reductase
- UniProt
- A9BHL2
- Ligands
- NAD
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydrodipicolinate reductase | protein | 342 | 32% helix, 27% strand | A9BHL2 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A
- EDO · 1,2-ethanediol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 455 | 0.66 | 0.79 | 38 | NAD, EDO |
| 2 | 56 | 0.30 | 0.76 | 13 | empty |
Compared structures
- 6G1H · Amine Dehydrogenase from Petrotoga mobilis; open form · 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 A9BHL2
- Elsewhere: RCSB PDB 6G1H · PDBe 6G1H · UniProt A9BHL2
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