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Crystal structure of bacterial reductase
Analyse Crystal structure of bacterial reductase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7CAW
- Type
- protein
- Length
- 941 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.876
- Source
- Acinetobacter baumannii
- Molecule
- 3-oxoacyl-ACP reductase FabG
- EC
- 1.1.1.100
- UniProt
- A0A1K1L6W4
- Pockets
- 4 · best druggability 0.86
Structure
x-ray diffraction · resolution 1.876 · 4 distinct chains · 50% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-oxoacyl-ACP reductase FabG (EC 1.1.1.100) | protein | 230 | 50% helix, 16% strand | A0A1K1L6W4 |
| B | 3-oxoacyl-ACP reductase FabG (EC 1.1.1.100) | protein | 241 | 51% helix, 15% strand | A0A1K1L6W4 |
| C | 3-oxoacyl-ACP reductase FabG (EC 1.1.1.100) | protein | 240 | 50% helix, 15% strand | A0A1K1L6W4 |
| D | 3-oxoacyl-ACP reductase FabG (EC 1.1.1.100) | protein | 230 | 50% helix, 16% strand | A0A1K1L6W4 |
Ligands and binding sites
- GOL · Glycerol · additive · 4 copies · chains B, D, A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1059 | 0.86 | 0.86 | 51 | empty |
| 2 | 1031 | 0.80 | 0.82 | 104 | GOL |
| 3 | 1064 | 0.79 | 0.81 | 107 | empty |
| 4 | 73 | 0.33 | 0.75 | 13 | empty |
Interfaces
6 interfaces between chains.
- A–C · 1732 Ų buried · 28 hydrogen bonds · protein-protein
- B–D · 1713 Ų buried · 30 hydrogen bonds · protein-protein
- A–D · 1497 Ų buried · 25 hydrogen bonds · protein-protein
- B–C · 1471 Ų buried · 25 hydrogen bonds · protein-protein
- C–D · 172 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 7CAW · Crystal structure of bacterial reductase · 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 A0A1K1L6W4
- Elsewhere: RCSB PDB 7CAW · PDBe 7CAW · UniProt A0A1K1L6W4
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