MolNFT v1 · #189932 · protein
Acetyl-CoA carboxylase-accb
7W5U · Acetyl-CoA carboxylase complex, beta-chain: “Acetyl-CoA carboxylase-accb”. X-ray diffraction, 1 ligand (SO4), 20 pockets (best druggability 0.83). MolNFT v1 #189932 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7W5U
- Type
- protein
- Length
- 3,078 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetyl-CoA carboxylase complex, beta-chain
- UniProt
- Q6ZZV4
- Ligands
- SO4
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Acetyl-CoA carboxylase complex, beta-chain | protein | 513 | 44% helix, 18% strand | Q6ZZV4 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 6 copies · chains A, F, B, E, D, C
- GOL · Glycerol · additive · 4 copies · chains B, E, C, A, D, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 1103 | 0.83 | 0.84 | 134 | SO4 |
| 2 | 868 | 0.81 | 0.84 | 99 | SO4 |
| 3 | 754 | 0.80 | 0.84 | 85 | SO4, GOL |
| 4 | 66 | 0.75 | 0.99 | 21 | empty |
| 5 | 64 | 0.74 | 0.99 | 24 | empty |
Interfaces
15 interfaces between chains.
- D–F · 4695 Ų buried · 60 hydrogen bonds · protein-protein
- B–E · 4564 Ų buried · 60 hydrogen bonds · protein-protein
- A–C · 4499 Ų buried · 61 hydrogen bonds · protein-protein
- B–C · 1186 Ų buried · 13 hydrogen bonds · protein-protein
- B–D · 1162 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 7W5U · Acetyl-CoA Carboxylase-AccB · the same entry in another collection · chain A against A, TM-score 1.00
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 Q6ZZV4
- Elsewhere: RCSB PDB 7W5U · PDBe 7W5U · UniProt Q6ZZV4
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