Research workbench
Crystal structure of domains AC3-AC5 of yeast acetyl-CoA carboxylase
Analyse Crystal structure of domains AC3-AC5 of yeast acetyl-CoA carboxylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CS4
- Type
- protein
- Length
- 787 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
- Pockets
- 12 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetyl-CoA carboxylase (EC 6.4.1.2, 6.3.4.14) | protein | 402 | 32% helix, 29% strand | Q00955 |
| B | Acetyl-CoA carboxylase (EC 6.4.1.2, 6.3.4.14) | protein | 385 | 33% helix, 27% strand | Q00955 |
Pockets
12 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 497 | 0.70 | 0.80 | 56 | empty |
| 2 | 311 | 0.64 | 0.80 | 41 | empty |
| 3 | 331 | 0.63 | 0.79 | 35 | empty |
| 4 | 54 | 0.58 | 0.92 | 18 | empty |
| 5 | 191 | 0.53 | 0.78 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 967 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 5CS4 · Crystal structure of domains AC3-AC5 of yeast acetyl-CoA carboxylase · 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 0.90
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 5CS4 · PDBe 5CS4 · UniProt Q00955
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