Research workbench
Crystal structure of beta-ketoacyl-acp synthase III
Analyse Crystal structure of beta-ketoacyl-acp synthase III in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HN9
- Type
- protein
- Length
- 634 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-ketoacyl-acyl carrier protein synthase III
- EC
- 2.3.1.41
- UniProt
- P0A6R0
- Ligands
- PO4
- Pockets
- 7 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Beta-ketoacyl-acyl carrier protein synthase III (EC 2.3.1.41) | protein | 317 | 40% helix, 27% strand | P0A6R0 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 319 | 0.80 | 0.91 | 54 | empty |
| 2 | 156 | 0.67 | 0.87 | 35 | empty |
| 3 | 158 | 0.66 | 0.86 | 31 | empty |
| 4 | 82 | 0.35 | 0.75 | 18 | empty |
| 5 | 80 | 0.34 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 2318 Ų buried · 43 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 P0A6R0
- Elsewhere: RCSB PDB 1HN9 · PDBe 1HN9 · UniProt P0A6R0
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