MolNFT v1 · #63622 · protein
Human ACC2 ct domain with cp-640186
3FF6 · Acetyl-CoA carboxylase 2: “Human ACC2 ct domain with cp-640186”. X-ray diffraction, 1 ligand (RCP), 20 pockets (best druggability 0.82). MolNFT v1 #63622 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3FF6
- Type
- protein
- Length
- 2,973 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetyl-CoA carboxylase 2
- EC
- 6.4.1.2, 6.3.4.14
- UniProt
- O00763
- Ligands
- RCP
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 4 distinct chains · 45% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetyl-CoA carboxylase 2 (EC 6.4.1.2, 6.3.4.14) | protein | 750 | 45% helix, 18% strand | O00763 |
| B | Acetyl-CoA carboxylase 2 (EC 6.4.1.2, 6.3.4.14) | protein | 748 | 45% helix, 19% strand | O00763 |
| C | Acetyl-CoA carboxylase 2 (EC 6.4.1.2, 6.3.4.14) | protein | 742 | 45% helix, 19% strand | O00763 |
| D | Acetyl-CoA carboxylase 2 (EC 6.4.1.2, 6.3.4.14) | protein | 733 | 45% helix, 19% strand | O00763 |
Ligands and binding sites
- RCP · (3R)-1'-(9-anthrylcarbonyl)-3-(morpholin-4-ylcarbonyl)-1,4'-bipiperidine · ligand · 4 copies · chains A, B, D, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1039 | 0.82 | 0.83 | 91 | empty |
| 2 | 724 | 0.82 | 0.85 | 63 | empty |
| 3 | 390 | 0.78 | 0.87 | 34 | empty |
| 4 | 470 | 0.76 | 0.84 | 62 | RCP |
| 5 | 431 | 0.74 | 0.84 | 61 | RCP |
Interfaces
6 interfaces between chains.
- A–B · 7204 Ų buried · 54 hydrogen bonds · protein-protein
- C–D · 6855 Ų buried · 57 hydrogen bonds · protein-protein
- A–C · 308 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 294 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 267 Ų buried · 1 hydrogen bond · 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 O00763
- Elsewhere: RCSB PDB 3FF6 · PDBe 3FF6 · UniProt O00763
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