Research workbench
Bc domain in the presence of citrate
Analyse Bc domain in the presence of citrate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HQ6
- Type
- protein
- Length
- 494 residues
- Chains
- 1
- 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
- Pockets
- 4 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetyl-CoA carboxylase 2 (EC 6.4.1.2, 6.3.4.14) | protein | 494 | 36% helix, 20% strand | O00763 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 933 | 0.70 | 0.75 | 93 | empty |
| 2 | 334 | 0.61 | 0.78 | 42 | empty |
| 3 | 182 | 0.51 | 0.77 | 26 | empty |
| 4 | 86 | 0.43 | 0.79 | 19 | empty |
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 4HQ6 · PDBe 4HQ6 · UniProt O00763
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