Research workbench
Engineered glycolyl-CoA reductase comprising 8 mutations with bound NADP+
Analyse Engineered glycolyl-CoA reductase comprising 8 mutations with bound NADP+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6GVS
- Type
- protein
- Length
- 4,406 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.579
- Source
- Rhodopseudomonas palustris BisB18
- Molecule
- Aldehyde dehydrogenase
- UniProt
- Q21A49
- Ligands
- NAP, K
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · resolution 2.579 · 2 distinct chains · 45% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, F, H, I | Aldehyde dehydrogenase | protein | 441 | 45% helix, 20% strand | Q21A49 |
| B, D, G, J | Aldehyde dehydrogenase | protein | 440 | 44% helix, 21% strand | Q21A49 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 10 copies · chains A, B, C, D, E, F, G, H, I, J
- K · Potassium ion · metal · 10 copies · chains A, B, C, D, E, F, G, H, I, J
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 948 | 0.81 | 0.83 | 100 | NAP |
| 2 | 493 | 0.81 | 0.87 | 56 | empty |
| 3 | 461 | 0.80 | 0.88 | 59 | empty |
| 4 | 408 | 0.80 | 0.89 | 53 | empty |
| 5 | 457 | 0.80 | 0.88 | 55 | empty |
Interfaces
17 interfaces between chains.
- G–H · 2508 Ų buried · 55 hydrogen bonds · protein-protein
- A–B · 2448 Ų buried · 50 hydrogen bonds · protein-protein
- E–F · 2442 Ų buried · 60 hydrogen bonds · protein-protein
- C–D · 2435 Ų buried · 45 hydrogen bonds · protein-protein
- B–C · 1222 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 6GVS · Engineered glycolyl-CoA reductase comprising 8 mutations with bound NADP+ · 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 Q21A49
- Elsewhere: RCSB PDB 6GVS · PDBe 6GVS · UniProt Q21A49
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.