MolNFT v1 · #56161 · protein
Crystal structure of S. pneumoniae enoyl-acyl carrier protein reductase (fabk)
2Z6I · Trans-2-enoyl-acp reductase II: “Crystal structure of S. pneumoniae enoyl-acyl carrier protein reductase (fabk)”. X-ray diffraction, 2 ligands (FMN, CA), 4 pockets (best druggability 0.78). MolNFT v1 #56161 on GenesisL1: 3D…
- PDB
- 2Z6I
- Type
- protein
- Length
- 638 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trans-2-enoyl-acp reductase II
- EC
- 1.3.1.9
- UniProt
- Q9FBC5
- Ligands
- FMN, CA
- Pockets
- 4 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trans-2-enoyl-acp reductase II (EC 1.3.1.9) | protein | 317 | 47% helix, 15% strand | Q9FBC5 |
| B | Trans-2-enoyl-acp reductase II (EC 1.3.1.9) | protein | 321 | 46% helix, 14% strand | Q9FBC5 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
- CA · Calcium ion · metal · 6 copies · chains A, B
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A
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 | 658 | 0.78 | 0.83 | 84 | CA, FMN |
| 2 | 639 | 0.76 | 0.82 | 79 | CA, FMN |
| 3 | 430 | 0.69 | 0.80 | 56 | empty |
| 4 | 64 | 0.32 | 0.76 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 2417 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 20 modified (engineered).
Compared structures
- 2Z6I · Crystal Structure of S. pneumoniae Enoyl-Acyl Carrier Protein Reductase (FabK) · 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 Q9FBC5
- Elsewhere: RCSB PDB 2Z6I · PDBe 2Z6I · UniProt Q9FBC5
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