Research workbench
Crystal structure of yeast acetyl-CoA carboxylase, unbiotinylated
Analyse Crystal structure of yeast acetyl-CoA carboxylase, unbiotinylated in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CSK
- Type
- protein
- Length
- 4,013 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
- 20 · best druggability 0.87
Structure
x-ray diffraction · 2 distinct chains · 40% 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 | 1996 | 41% helix, 21% strand | Q00955 |
| B | Acetyl-CoA carboxylase (EC 6.4.1.2, 6.3.4.14) | protein | 2017 | 40% helix, 20% strand | Q00955 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 641 | 0.87 | 0.91 | 75 | empty |
| 2 | 633 | 0.86 | 0.91 | 81 | empty |
| 3 | 871 | 0.84 | 0.86 | 85 | empty |
| 4 | 205 | 0.81 | 0.94 | 35 | empty |
| 5 | 795 | 0.79 | 0.83 | 72 | empty |
Interfaces
1 interface between chains.
- A–B · 9264 Ų buried · 106 hydrogen bonds · protein-protein
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 5CSK · PDBe 5CSK · UniProt Q00955
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