Research workbench
2.30 ångström resolution crystal structure of betaine aldehyde dehydrogenase (betb) from staphylococcus aureus with bme-free CYS289
Analyse 2.30 ångström resolution crystal structure of betaine aldehyde dehydrogenase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4NU9
- Type
- protein
- Length
- 997 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Betaine aldehyde dehydrogenase
- EC
- 1.2.1.8
- UniProt
- Q5HCU0
- Ligands
- NA
- Pockets
- 8 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Betaine aldehyde dehydrogenase (EC 1.2.1.8) | protein | 501 | 42% helix, 21% strand | Q5HCU0 |
| B | Betaine aldehyde dehydrogenase (EC 1.2.1.8) | protein | 496 | 41% helix, 21% strand | Q5HCU0 |
Ligands and binding sites
- NA · Sodium ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 452 | 0.66 | 0.78 | 61 | empty |
| 2 | 348 | 0.63 | 0.79 | 45 | empty |
| 3 | 69 | 0.62 | 0.91 | 20 | empty |
| 4 | 189 | 0.50 | 0.77 | 24 | empty |
| 5 | 140 | 0.44 | 0.76 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 755 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 4NU9 · 2.30 Angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betB) from… · 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 Q5HCU0
- Elsewhere: RCSB PDB 4NU9 · PDBe 4NU9 · UniProt Q5HCU0
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