MolNFT v1 · #32727 · protein
Structure of E.COLI kas I H298Q mutant in complex with C12 fatty acid
2BYZ · 3-oxoacyl-[acyl-carrier-protein] synthase I: “Structure of E.COLI kas I H298Q mutant in complex with C12 fatty acid”. X-ray diffraction, 2 ligands (DAO, NH4), 12 pockets (best druggability 0.77). MolNFT v1 #32727 on GenesisL1: 3D…
- PDB
- 2BYZ
- Type
- protein
- Length
- 1,620 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
- DAO, NH4
- Pockets
- 12 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 37% 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 | 405 | 37% helix, 22% strand | P14926 |
Ligands and binding sites
- DAO · Lauric acid · ligand · 4 copies · chains A, B, C, D
- NH4 · Ammonium ion · ion · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 260 | 0.77 | 0.90 | 53 | DAO |
| 2 | 277 | 0.75 | 0.88 | 48 | DAO |
| 3 | 269 | 0.73 | 0.87 | 51 | DAO |
| 4 | 57 | 0.70 | 0.97 | 17 | DAO |
| 5 | 189 | 0.66 | 0.85 | 37 | empty |
Interfaces
3 interfaces between chains.
- C–D · 2997 Ų buried · 54 hydrogen bonds · protein-protein
- A–B · 2970 Ų buried · 50 hydrogen bonds · protein-protein
- A–C · 382 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 4 covalent (covalent ligand).
Compared structures
- 2BYZ · Structure of E.coli KAS I H298Q mutant in complex with C12 fatty acid · 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 2BYZ · PDBe 2BYZ · UniProt P14926
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