MolNFT v1 · #91431 · protein
Crystal structure of apo-formed YMTOAR1
4FD3 · 3-oxoacyl-[acyl-carrier-protein] reductase: “Crystal structure of apo-formed YMTOAR1”. X-ray diffraction, 17 pockets (best druggability 0.76). MolNFT v1 #91431 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4FD3
- Type
- protein
- Length
- 1,521 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3-oxoacyl-[acyl-carrier-protein] reductase
- EC
- 1.1.1.100
- UniProt
- P35731
- Pockets
- 17 · best druggability 0.76
Structure
x-ray diffraction · 6 distinct chains · 44% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) | protein | 254 | 43% helix, 22% strand | P35731 |
| B | 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) | protein | 253 | 44% helix, 21% strand | P35731 |
| C | 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) | protein | 250 | 46% helix, 20% strand | P35731 |
| D | 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) | protein | 268 | 44% helix, 19% strand | P35731 |
| E | 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) | protein | 250 | 44% helix, 21% strand | P35731 |
| F | 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) | protein | 246 | 46% helix, 20% strand | P35731 |
Pockets
17 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 444 | 0.76 | 0.85 | 53 | empty |
| 2 | 662 | 0.74 | 0.80 | 52 | empty |
| 3 | 275 | 0.71 | 0.85 | 41 | empty |
| 4 | 250 | 0.71 | 0.86 | 36 | empty |
| 5 | 140 | 0.61 | 0.85 | 35 | empty |
Interfaces
10 interfaces between chains.
- A–D · 1620 Ų buried · 26 hydrogen bonds · protein-protein
- B–E · 1607 Ų buried · 22 hydrogen bonds · protein-protein
- A–C · 595 Ų buried · 10 hydrogen bonds · protein-protein
- C–E · 593 Ų buried · 11 hydrogen bonds · protein-protein
- A–E · 563 Ų buried · 9 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 P35731
- Elsewhere: RCSB PDB 4FD3 · PDBe 4FD3 · UniProt P35731
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