Research workbench
Acetyl-CoA carboxylase carboxyltransferase domain
Analyse Acetyl-CoA carboxylase carboxyltransferase domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OD2
- Type
- protein
- Length
- 1,414 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetyl-coenzyme a carboxylase
- EC
- 6.4.1.2
- UniProt
- Q00955
- Ligands
- ACO, ADE
- Pockets
- 15 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetyl-coenzyme a carboxylase (EC 6.4.1.2) | protein | 719 | 41% helix, 20% strand | Q00955 |
| B | Acetyl-coenzyme a carboxylase (EC 6.4.1.2) | protein | 695 | 41% helix, 19% strand | Q00955 |
Ligands and binding sites
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 | 764 | 0.81 | 0.84 | 63 | empty |
| 2 | 514 | 0.77 | 0.84 | 36 | empty |
| 3 | 477 | 0.75 | 0.83 | 55 | ADE |
| 4 | 569 | 0.73 | 0.81 | 59 | ACO |
| 5 | 192 | 0.61 | 0.82 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 5762 Ų buried · 51 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 34 modified (engineered).
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 Q00955
- Elsewhere: RCSB PDB 1OD2 · PDBe 1OD2 · UniProt Q00955
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