Research workbench
Crystal structure of a bacterial ketosynthase
Analyse Crystal structure of a bacterial ketosynthase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7F28
- Type
- protein
- Length
- 1,181 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- KETOACYL_SYNTH_N domain-containing protein; Putative 3-oxoacyl-[acp] synthase fabv
- EC
- 2.3.1.41
- UniProt
- A0A0E1PUF7, A0A0E1Q0H1
- Pockets
- 17 · best druggability 0.80
Structure
x-ray diffraction · 3 distinct chains · 37% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | KETOACYL_SYNTH_N domain-containing protein | protein | 203 | 36% helix, 22% strand | A0A0E1PUF7 |
| B, D | Putative 3-oxoacyl-[acp] synthase fabv (EC 2.3.1.41) | protein | 390 | 38% helix, 24% strand | A0A0E1Q0H1 |
| C | KETOACYL_SYNTH_N domain-containing protein | protein | 198 | 37% helix, 23% strand | A0A0E1PUF7 |
Pockets
17 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 153 | 0.80 | 0.96 | 29 | empty |
| 2 | 149 | 0.80 | 0.96 | 28 | empty |
| 3 | 117 | 0.69 | 0.91 | 27 | empty |
| 4 | 146 | 0.68 | 0.88 | 30 | empty |
| 5 | 518 | 0.64 | 0.77 | 61 | empty |
Interfaces
3 interfaces between chains.
- C–D · 2450 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 2443 Ų buried · 20 hydrogen bonds · protein-protein
- A–D · 459 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 7F28 · Crystal structure of a bacterial ketosynthase · 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 A0A0E1PUF7
- Every structure of UniProt A0A0E1Q0H1
- Elsewhere: RCSB PDB 7F28 · PDBe 7F28 · UniProt A0A0E1PUF7 · UniProt A0A0E1Q0H1
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