Research workbench
Crystal structure of enoyl-[acyl-carrier-protein] reductase inha from mycobacterium abscessus in complex with NAD
Analyse Crystal structure of enoyl-[acyl-carrier-protein] reductase inha from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7L6C
- Type
- protein
- Length
- 1,067 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
- B1MC30
- Ligands
- NAD, NA
- Pockets
- 15 · best druggability 0.84
Structure
x-ray diffraction · 3 distinct chains · 47% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 267 | 47% helix, 16% strand | B1MC30 |
| B | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 268 | 47% helix, 16% strand | B1MC30 |
| D | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 265 | 47% helix, 17% strand | B1MC30 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 4 copies · chains A, B, C, D
- NA · Sodium ion · metal · 4 copies · chains A, B, C, D
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1165 | 0.84 | 0.85 | 54 | empty |
| 2 | 516 | 0.81 | 0.87 | 52 | NAD, EDO |
| 3 | 474 | 0.81 | 0.88 | 48 | NAD |
| 4 | 406 | 0.79 | 0.88 | 45 | NAD |
| 5 | 683 | 0.77 | 0.82 | 54 | NAD |
Interfaces
6 interfaces between chains.
- A–B · 1606 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 1580 Ų buried · 12 hydrogen bonds · protein-protein
- B–D · 1458 Ų buried · 19 hydrogen bonds · protein-protein
- A–C · 1451 Ų buried · 19 hydrogen bonds · protein-protein
- A–D · 672 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 7L6C · Crystal Structure of Enoyl-[acyl-carrier-protein] reductase InhA from Mycobacterium… · 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 B1MC30
- Elsewhere: RCSB PDB 7L6C · PDBe 7L6C · UniProt B1MC30
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