Research workbench
Crystal structure of the biotin carboxylase subunit, E296A mutant, of acetyl-CoA carboxylase from escherichia COLI
Analyse Crystal structure of the biotin carboxylase subunit, E296A mutant, of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3G8D
- Type
- protein
- Length
- 817 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Biotin carboxylase
- EC
- 6.3.4.14, 6.4.1.2
- UniProt
- P24182
- Ligands
- ADP, MG, SO4
- Pockets
- 5 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Biotin carboxylase (EC 6.3.4.14, 6.4.1.2) | protein | 373 | 35% helix, 29% strand | P24182 |
| B | Biotin carboxylase (EC 6.3.4.14, 6.4.1.2) | protein | 444 | 36% helix, 26% strand | P24182 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains B
- MG · Magnesium ion · metal · chains B
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 354 | 0.75 | 0.86 | 47 | empty |
| 2 | 767 | 0.74 | 0.79 | 74 | ADP, MG, SO4 |
| 3 | 134 | 0.68 | 0.89 | 33 | empty |
| 4 | 60 | 0.65 | 0.94 | 19 | empty |
| 5 | 343 | 0.61 | 0.78 | 49 | SO4 |
Interfaces
1 interface between chains.
- A–B · 1358 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 3G8D · Crystal structure of the biotin carboxylase subunit, E296A mutant, of acetyl-COA… · the same entry in another collection · chain A against A, TM-score 1.00
- P24182 · AlphaFold monomer V2.0 prediction for biotin carboxylase (P24182) · a predicted model of the same protein · 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 P24182
- Elsewhere: RCSB PDB 3G8D · PDBe 3G8D · UniProt P24182
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