Research workbench
Apo structure of aldehyde dehydrogenase from bacillus cereus
Analyse Apo structure of aldehyde dehydrogenase from bacillus cereus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5GT6
- Type
- protein
- Length
- 1,958 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Betaine-aldehyde dehydrogenase
- UniProt
- A0A150BLG9
- Ligands
- NA
- Pockets
- 19 · best druggability 0.89
Structure
x-ray diffraction · 3 distinct chains · 42% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Betaine-aldehyde dehydrogenase | protein | 491 | 42% helix, 21% strand | A0A150BLG9 |
| B | Betaine-aldehyde dehydrogenase | protein | 489 | 42% helix, 22% strand | A0A150BLG9 |
| C | Betaine-aldehyde dehydrogenase | protein | 487 | 43% helix, 21% strand | A0A150BLG9 |
Ligands and binding sites
- NA · Sodium ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1128 | 0.89 | 0.90 | 132 | empty |
| 2 | 402 | 0.83 | 0.91 | 60 | empty |
| 3 | 406 | 0.77 | 0.87 | 41 | empty |
| 4 | 221 | 0.77 | 0.91 | 33 | empty |
| 5 | 781 | 0.76 | 0.80 | 96 | empty |
Interfaces
6 interfaces between chains.
- A–D · 2675 Ų buried · 48 hydrogen bonds · protein-protein
- B–C · 2672 Ų buried · 45 hydrogen bonds · protein-protein
- A–B · 1155 Ų buried · 16 hydrogen bonds · protein-protein
- C–D · 1127 Ų buried · 20 hydrogen bonds · protein-protein
- B–D · 1113 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 5GT6 · Apo structure of Aldehyde Dehydrogenase from Bacillus cereus · 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 A0A150BLG9
- Elsewhere: RCSB PDB 5GT6 · PDBe 5GT6 · UniProt A0A150BLG9
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