Research workbench
Crystal structure of tabtoxin resistance protein complexed with an acyl coenzyme a
Analyse Crystal structure of tabtoxin resistance protein complexed with an acyl… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GHE
- Type
- protein
- Length
- 341 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetyltransferase
- EC
- 2.3.1.-
- UniProt
- P16966
- Ligands
- ACO
- Pockets
- 2 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetyltransferase (EC 2.3.1.-) | protein | 170 | 34% helix, 35% strand | P16966 |
| B | Acetyltransferase (EC 2.3.1.-) | protein | 171 | 35% helix, 35% strand | P16966 |
Ligands and binding sites
- ACO · Acetyl coenzyme *A · ligand · 2 copies · chains A, 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 733 | 0.75 | 0.80 | 66 | ACO |
| 2 | 329 | 0.62 | 0.78 | 38 | ACO |
Interfaces
1 interface between chains.
- A–B · 388 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 1GHE · Crystal structure of tabtoxin resistance protein complexed with an acyl coenzyme a · the same entry in another collection · chain A against A, TM-score 1.00
- P16966 · AlphaFold monomer V2.0 prediction for acetyltransferase (P16966) · 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 P16966
- Elsewhere: RCSB PDB 1GHE · PDBe 1GHE · UniProt P16966
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