MolNFT v1 · #24557 · protein
Acetyl-CoA carboxylase carboxyltransferase domain in complex with inhibitor haloxyfop
1UYS: “Acetyl-CoA carboxylase carboxyltransferase domain in complex with inhibitor haloxyfop”. X-ray diffraction, 1 ligand (H1L), 20 pockets (best druggability 0.79). MolNFT v1 #24557 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 1UYS
- Type
- protein
- Length
- 1,997 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetyl-CoA carboxylase
- EC
- 6.4.1.2
- UniProt
- Q00955
- Ligands
- H1L
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Acetyl-CoA carboxylase (EC 6.4.1.2) | protein | 669 | 38% helix, 23% strand | Q00955 |
| C | Acetyl-CoA carboxylase (EC 6.4.1.2) | protein | 659 | 39% helix, 19% strand | Q00955 |
Ligands and binding sites
- H1L · (2R)-2-(4-{[3-chloro-5-(trifluoromethyl)pyridin-2-yl]oxy}phenoxy)propanoic acid · ligand · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 887 | 0.79 | 0.81 | 88 | H1L |
| 2 | 782 | 0.79 | 0.82 | 71 | empty |
| 3 | 834 | 0.78 | 0.81 | 87 | H1L |
| 4 | 562 | 0.68 | 0.78 | 35 | empty |
| 5 | 213 | 0.62 | 0.82 | 30 | empty |
Interfaces
2 interfaces between chains.
- B–C · 4724 Ų buried · 40 hydrogen bonds · protein-protein
- A–B · 1158 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 48 modified (engineered).
Compared structures
- 1UYS · Acetyl-CoA carboxylase carboxyltransferase domain in complex with inhibitor haloxyfop · the same entry in another collection · chain A against A, TM-score 1.00
- Q00955 · AlphaFold monomer V2.0 prediction for acetyl-CoA carboxylase (Q00955) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 Q00955
- Elsewhere: RCSB PDB 1UYS · PDBe 1UYS · UniProt Q00955
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