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The biotin carboxylase (bc) domain of human acetyl-CoA carboxylase 2 (ACC2) in complex with soraphen a
Analyse The biotin carboxylase (bc) domain of human acetyl-CoA carboxylase 2 (ACC2) in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3GID
- Type
- protein
- Length
- 917 residues
- Chains
- 2
- 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
- S1A
- Pockets
- 13 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetyl-CoA carboxylase 2 (EC 6.4.1.2, 6.3.4.14) | protein | 460 | 37% helix, 23% strand | O00763 |
| B | Acetyl-CoA carboxylase 2 (EC 6.4.1.2, 6.3.4.14) | protein | 457 | 37% helix, 22% strand | O00763 |
Ligands and binding sites
- S1A · Soraphen A · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 625 | 0.79 | 0.84 | 57 | empty |
| 2 | 370 | 0.70 | 0.82 | 54 | empty |
| 3 | 357 | 0.65 | 0.79 | 42 | S1A |
| 4 | 400 | 0.64 | 0.78 | 44 | S1A |
| 5 | 231 | 0.51 | 0.76 | 32 | empty |
Interfaces
1 interface between chains.
- A–B · 1217 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 3GID · The biotin carboxylase (BC) domain of human Acetyl-CoA Carboxylase 2 (ACC2) in complex… · the same entry in another collection · chain A against A, TM-score 1.00
- O00763 · AlphaFold monomer V2.0 prediction for acetyl-CoA carboxylase 2 (O00763) · a predicted model of the same protein · chain B against A, TM-score 0.93
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 3GID · PDBe 3GID · UniProt O00763
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