Research workbench
The crystal structure of the carboxyltransferase subunit of acc from escherichia COLI
Analyse The crystal structure of the carboxyltransferase subunit of acc from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2F9Y
- Type
- protein
- Length
- 558 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetyl-CoA carboxylase, carboxyltransferase alpha chain; Acetyl-coenzyme a carboxylase…
- EC
- 6.4.1.2
- UniProt
- P0A9Q6
- Ligands
- ZN
- Pockets
- 2 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetyl-CoA carboxylase, carboxyltransferase alpha chain (EC 6.4.1.2) | protein | 301 | 44% helix, 15% strand | — |
| B | Acetyl-coenzyme a carboxylase carboxyl transferase subunit beta (EC 6.4.1.2) | protein | 257 | 35% helix, 20% strand | P0A9Q6 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 452 | 0.64 | 0.77 | 41 | empty |
| 2 | 66 | 0.47 | 0.84 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 2105 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 2F9Y · The Crystal Structure of The Carboxyltransferase Subunit of ACC from Escherichia coli · the same entry in another collection · chain A against A, TM-score 1.00
- P0A9Q6 · AlphaFold monomer V2.0 prediction for acetyl-coenzyme a carboxylase carboxyl transferase… · a predicted model of the same protein · chain B against A, TM-score 0.99
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 P0A9Q6
- Elsewhere: RCSB PDB 2F9Y · PDBe 2F9Y · UniProt P0A9Q6
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