Research workbench
Acetyl-CoA carboxylase carboxyltransferase domain L1705I/ V1967I mutant
Analyse Acetyl-CoA carboxylase carboxyltransferase domain L1705I/ V1967I mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UYV
- Type
- protein
- Length
- 1,693 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
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 3 distinct chains · 38% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetyl-CoA carboxylase (EC 6.4.1.2) | protein | 571 | 39% helix, 21% strand | Q00955 |
| B | Acetyl-CoA carboxylase (EC 6.4.1.2) | protein | 552 | 39% helix, 20% strand | Q00955 |
| C | Acetyl-CoA carboxylase (EC 6.4.1.2) | protein | 570 | 37% helix, 21% strand | Q00955 |
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1046 | 0.82 | 0.83 | 106 | empty |
| 2 | 493 | 0.76 | 0.84 | 37 | empty |
| 3 | 649 | 0.70 | 0.78 | 50 | empty |
| 4 | 390 | 0.68 | 0.80 | 43 | empty |
| 5 | 223 | 0.61 | 0.81 | 29 | empty |
Interfaces
2 interfaces between chains.
- B–C · 3035 Ų buried · 26 hydrogen bonds · protein-protein
- A–B · 1270 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 1UYV · Acetyl-CoA carboxylase carboxyltransferase domain L1705I/V1967I mutant · 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 A 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 1UYV · PDBe 1UYV · UniProt Q00955
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