Research workbench
Crystal structure of the carboxyltransferase domain of acetyl-coenzyme a carboxylase in complex with compound 2
Analyse Crystal structure of the carboxyltransferase domain of acetyl-coenzyme a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3H0J
- Type
- protein
- Length
- 2,021 residues
- Chains
- 3
- 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
- B36
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · 3 distinct chains · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetyl-CoA carboxylase (EC 6.4.1.2, 6.3.4.14) | protein | 681 | 38% helix, 21% strand | Q00955 |
| B | Acetyl-CoA carboxylase (EC 6.4.1.2, 6.3.4.14) | protein | 675 | 38% helix, 23% strand | Q00955 |
| C | Acetyl-CoA carboxylase (EC 6.4.1.2, 6.3.4.14) | protein | 665 | 39% helix, 20% strand | Q00955 |
Ligands and binding sites
- B36 · 6-{[1-(anthracen-9-ylcarbonyl)piperidin-4-yl]methyl}-2-methylquinoline · 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, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1010 | 0.84 | 0.85 | 95 | B36 |
| 2 | 515 | 0.77 | 0.84 | 36 | empty |
| 3 | 460 | 0.75 | 0.83 | 47 | B36 |
| 4 | 686 | 0.73 | 0.79 | 55 | empty |
| 5 | 240 | 0.62 | 0.81 | 40 | empty |
Interfaces
2 interfaces between chains.
- B–C · 5693 Ų buried · 48 hydrogen bonds · protein-protein
- A–B · 1282 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 3H0J · Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase in… · 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 C 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 3H0J · PDBe 3H0J · UniProt Q00955
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