Research workbench
Human mitochondrial beta-ketoacyl acp synthase
Analyse Human mitochondrial beta-ketoacyl acp synthase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IWY
- Type
- protein
- Length
- 843 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3-oxoacyl-[acyl-carrier-protein] synthase
- EC
- 2.3.1.41
- UniProt
- Q9NWU1
- Ligands
- NH4
- Pockets
- 11 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41) | protein | 420 | 39% helix, 22% strand | Q9NWU1 |
| B | 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41) | protein | 423 | 39% helix, 22% strand | Q9NWU1 |
Ligands and binding sites
- NH4 · Ammonium ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 219 | 0.73 | 0.88 | 34 | empty |
| 2 | 82 | 0.72 | 0.96 | 22 | empty |
| 3 | 388 | 0.69 | 0.81 | 37 | empty |
| 4 | 146 | 0.44 | 0.76 | 24 | empty |
| 5 | 120 | 0.43 | 0.77 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 3576 Ų buried · 47 hydrogen bonds · protein-protein
Compared structures
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 Q9NWU1
- Elsewhere: RCSB PDB 2IWY · PDBe 2IWY · UniProt Q9NWU1
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