Research workbench
Crystal structure of human-yeast chimera acetyl CoA carboxylase ct domain bound to compound 6
Analyse Crystal structure of human-yeast chimera acetyl CoA carboxylase ct domain bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4WZ8
- Type
- protein
- Length
- 1,396 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetyl-CoA carboxylase
- EC
- 6.4.1.2, 6.3.4.14
- UniProt
- Q00955
- Ligands
- 3W7
- Pockets
- 15 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Acetyl-CoA carboxylase (EC 6.4.1.2, 6.3.4.14) | protein | 698 | 40% helix, 20% strand | Q00955 |
| C | Acetyl-CoA carboxylase (EC 6.4.1.2, 6.3.4.14) | protein | 698 | 41% helix, 20% strand | Q00955 |
Ligands and binding sites
- 3W7 · 1'-(2H-indazol-5-ylcarbonyl)-1-(propan-2-yl)-1,4-dihydrospiro[indazole-5,4'-piperidin]-7(6H)-one · ligand · 2 copies · chains B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 680 | 0.82 | 0.86 | 63 | empty |
| 2 | 465 | 0.76 | 0.84 | 52 | 3W7 |
| 3 | 463 | 0.76 | 0.85 | 38 | empty |
| 4 | 454 | 0.75 | 0.84 | 51 | 3W7 |
| 5 | 306 | 0.60 | 0.78 | 45 | empty |
Interfaces
1 interface between chains.
- B–C · 6080 Ų buried · 49 hydrogen bonds · protein-protein
Compared structures
- 4WZ8 · Crystal structure of human-yeast chimera acetyl coA carboxylase CT domain bound to… · the same entry in another collection · chain B against B, 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 0.99
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 4WZ8 · PDBe 4WZ8 · UniProt Q00955
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