Research workbench
Putative fabg bound to NADH from acinetobacter baumannii
Analyse Putative fabg bound to NADH from acinetobacter baumannii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7KRM
- Type
- protein
- Length
- 956 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3-oxoacyl-[acyl-carrier-protein] reductase
- EC
- 1.1.1.47
- UniProt
- A0A077GFB1
- Ligands
- NAD
- Pockets
- 13 · best druggability 0.85
Structure
x-ray diffraction · 4 distinct chains · 49% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.47) | protein | 240 | 50% helix, 16% strand | A0A077GFB1 |
| B | 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.47) | protein | 235 | 49% helix, 17% strand | A0A077GFB1 |
| C | 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.47) | protein | 244 | 48% helix, 17% strand | A0A077GFB1 |
| D | 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.47) | protein | 237 | 49% helix, 17% strand | A0A077GFB1 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 439 | 0.85 | 0.92 | 50 | empty |
| 2 | 487 | 0.68 | 0.79 | 47 | NAD |
| 3 | 526 | 0.65 | 0.77 | 55 | empty |
| 4 | 309 | 0.62 | 0.79 | 34 | NAD |
| 5 | 307 | 0.60 | 0.78 | 37 | NAD |
Interfaces
6 interfaces between chains.
- A–D · 1654 Ų buried · 28 hydrogen bonds · protein-protein
- B–C · 1642 Ų buried · 33 hydrogen bonds · protein-protein
- A–B · 1615 Ų buried · 20 hydrogen bonds · protein-protein
- C–D · 1613 Ų buried · 19 hydrogen bonds · protein-protein
- B–D · 233 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 7KRM · Putative FabG bound to NADH from Acinetobacter baumannii · 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 A0A077GFB1
- Elsewhere: RCSB PDB 7KRM · PDBe 7KRM · UniProt A0A077GFB1
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