MolNFT v1 · #149500 · protein
Citrate-induced acetyl-CoA carboxylase (acc-cit) filament at 5.4 a resolution
6G2D · Acetyl-CoA carboxylase 1: “Citrate-induced acetyl-CoA carboxylase (acc-cit) filament at 5.4 a resolution”. Electron microscopy, 20 pockets (best druggability 0.87). MolNFT v1 #149500 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6G2D
- Type
- protein
- Length
- 5,501 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetyl-CoA carboxylase 1
- EC
- 6.4.1.2, 6.3.4.14
- UniProt
- Q13085
- Pockets
- 20 · best druggability 0.87
Structure
electron microscopy · 3 distinct chains · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Acetyl-CoA carboxylase 1 (EC 6.4.1.2, 6.3.4.14) | protein | 625 | 45% helix, 15% strand | Q13085 |
| C, D | Acetyl-CoA carboxylase 1 (EC 6.4.1.2, 6.3.4.14) | protein | 2121 | 41% helix, 19% strand | Q13085 |
| F | Acetyl-CoA carboxylase 1 (EC 6.4.1.2, 6.3.4.14) | protein | 634 | 45% helix, 15% strand | Q13085 |
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 | 760 | 0.87 | 0.90 | 88 | empty |
| 2 | 1036 | 0.87 | 0.87 | 108 | empty |
| 3 | 1036 | 0.85 | 0.86 | 133 | empty |
| 4 | 573 | 0.85 | 0.90 | 72 | empty |
| 5 | 904 | 0.84 | 0.86 | 114 | empty |
Interfaces
3 interfaces between chains.
- C–D · 11162 Ų buried · 70 hydrogen bonds · protein-protein
- B–D · 1594 Ų buried · 17 hydrogen bonds · protein-protein
- C–F · 1586 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 6G2D · Citrate-induced acetyl-CoA carboxylase (ACC-Cit) filament at 5.4 A resolution · the same entry in another collection · chain F against F, TM-score 1.00
- Q13085 · AlphaFold monomer V2.0 prediction for acetyl-CoA carboxylase 1 (Q13085) · a predicted model of the same protein · chain C against A, TM-score 0.94
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 Q13085
- Elsewhere: RCSB PDB 6G2D · PDBe 6G2D · UniProt Q13085
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