MolNFT v1 · #114718 · protein
ABYA1 - tetronic acid condensing enzyme
5BY7 · 3-oxoacyl-acp synthase III: “ABYA1 - tetronic acid condensing enzyme”. X-ray diffraction, 12 pockets (best druggability 0.83). MolNFT v1 #114718 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5BY7
- Type
- protein
- Length
- 1,270 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3-oxoacyl-acp synthase III
- UniProt
- F4F7F9
- Pockets
- 12 · best druggability 0.83
Structure
x-ray diffraction · 4 distinct chains · 36% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-oxoacyl-acp synthase III | protein | 337 | 37% helix, 26% strand | F4F7F9 |
| B | 3-oxoacyl-acp synthase III | protein | 321 | 37% helix, 27% strand | F4F7F9 |
| C | 3-oxoacyl-acp synthase III | protein | 310 | 36% helix, 26% strand | F4F7F9 |
| D | 3-oxoacyl-acp synthase III | protein | 302 | 35% helix, 27% strand | F4F7F9 |
Pockets
12 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 447 | 0.83 | 0.90 | 42 | empty |
| 2 | 1137 | 0.82 | 0.83 | 107 | empty |
| 3 | 491 | 0.80 | 0.86 | 56 | empty |
| 4 | 497 | 0.77 | 0.85 | 51 | empty |
| 5 | 233 | 0.55 | 0.78 | 25 | empty |
Interfaces
5 interfaces between chains.
- A–D · 2747 Ų buried · 50 hydrogen bonds · protein-protein
- B–C · 2731 Ų buried · 44 hydrogen bonds · protein-protein
- A–B · 317 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 258 Ų buried · 0 hydrogen bonds · protein-protein
- B–D · 177 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 5BY7 · AbyA1 - tetronic acid condensing enzyme · 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 F4F7F9
- Elsewhere: RCSB PDB 5BY7 · PDBe 5BY7 · UniProt F4F7F9
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