MolNFT v1 · #154165 · protein
NAD+ bound structure of enoyl-acyl carrier protein reductase (fabi) from acinetobacter baumanii
6K23 · Enoyl-[acyl-carrier-protein] reductase [NADH]: “NAD+ bound structure of enoyl-acyl carrier protein reductase (fabi) from acinetobacter baumanii”. X-ray diffraction, 1 ligand (NAD), 13 pockets (best druggability 0.85). MolNFT v1…
- PDB
- 6K23
- Type
- protein
- Length
- 1,040 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enoyl-[acyl-carrier-protein] reductase [NADH]
- EC
- 1.3.1.9
- UniProt
- V5VH25
- Ligands
- NAD
- Pockets
- 13 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 260 | 49% helix, 14% strand | V5VH25 |
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, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1045 | 0.85 | 0.85 | 44 | empty |
| 2 | 888 | 0.81 | 0.82 | 75 | NAD |
| 3 | 916 | 0.81 | 0.82 | 79 | NAD |
| 4 | 634 | 0.79 | 0.84 | 44 | NAD |
| 5 | 683 | 0.79 | 0.83 | 46 | NAD |
Interfaces
6 interfaces between chains.
- B–D · 1777 Ų buried · 37 hydrogen bonds · protein-protein
- A–C · 1762 Ų buried · 42 hydrogen bonds · protein-protein
- C–D · 1363 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 1363 Ų buried · 16 hydrogen bonds · protein-protein
- A–D · 642 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 6K23 · NAD+ bound structure of enoyl-acyl carrier protein reductase (FabI) from Acinetobacter… · 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 V5VH25
- Elsewhere: RCSB PDB 6K23 · PDBe 6K23 · UniProt V5VH25
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