MolNFT v1 · #148889 · protein
Structure and function of aldehyde dehydrogenase from thermus thermophilus: an enzyme with an evolutionarily-distinct C-terminal arm (native protein)
6FJX: “Structure and function of aldehyde dehydrogenase from thermus thermophilus: an enzyme with an…”. X-ray diffraction, 1 ligand (SO4), 12 pockets (best druggability 0.73). MolNFT v1 #148889 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6FJX
- Type
- protein
- Length
- 1,058 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aldehyde dehydrogenase
- EC
- 1.2.1.3
- UniProt
- Q72KD3
- Ligands
- SO4
- Pockets
- 12 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Aldehyde dehydrogenase (EC 1.2.1.3) | protein | 529 | 40% helix, 20% strand | Q72KD3 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 6 copies · chains A, B
- BOG · octyl beta-D-glucopyranoside · additive · 2 copies · chains A, B
- PGE · Triethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 636 | 0.73 | 0.80 | 86 | SO4 |
| 2 | 60 | 0.73 | 0.98 | 24 | SO4 |
| 3 | 69 | 0.72 | 0.97 | 28 | SO4 |
| 4 | 469 | 0.70 | 0.80 | 41 | empty |
| 5 | 362 | 0.66 | 0.80 | 47 | SO4 |
Interfaces
1 interface between chains.
- A–B · 3740 Ų buried · 59 hydrogen bonds · protein-protein
Compared structures
- 6FJX · Structure and function of aldehyde dehydrogenase from Thermus thermophilus: An enzyme… · 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 Q72KD3
- Elsewhere: RCSB PDB 6FJX · PDBe 6FJX · UniProt Q72KD3
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