MolNFT v1 · #32724 · protein
Structure of escherichia COLI beta-ketoacyl (acyl carrier protein) synthase I LYS328ALA mutant
2BYW · 3-oxoacyl-[acyl-carrier-protein] synthase I: “Structure of escherichia COLI beta-ketoacyl (acyl carrier protein) synthase I LYS328ALA mutant”. X-ray diffraction, 1 ligand (NH4), 9 pockets (best druggability 0.67). MolNFT v1 #32724…
- PDB
- 2BYW
- Type
- protein
- Length
- 1,624 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3-oxoacyl-[acyl-carrier-protein] synthase I
- EC
- 2.3.1.41
- UniProt
- P14926
- Ligands
- NH4
- Pockets
- 9 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | 3-oxoacyl-[acyl-carrier-protein] synthase I (EC 2.3.1.41) | protein | 406 | 38% helix, 22% strand | P14926 |
Ligands and binding sites
- NH4 · Ammonium ion · ion · 8 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 186 | 0.67 | 0.86 | 38 | empty |
| 2 | 174 | 0.66 | 0.85 | 32 | empty |
| 3 | 173 | 0.64 | 0.85 | 37 | empty |
| 4 | 137 | 0.61 | 0.85 | 38 | empty |
| 5 | 239 | 0.48 | 0.74 | 28 | empty |
Interfaces
3 interfaces between chains.
- C–D · 2987 Ų buried · 56 hydrogen bonds · protein-protein
- A–B · 2963 Ų buried · 51 hydrogen bonds · protein-protein
- A–D · 134 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 2BYW · Structure of Escherichia coli beta-ketoacyl (acyl carrier protein) synthase I LYS328ALA… · 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 P14926
- Elsewhere: RCSB PDB 2BYW · PDBe 2BYW · UniProt P14926
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