Research workbench
Phosphotransacetylase from methanosarcina thermophila soaked with coenzyme a
Analyse Phosphotransacetylase from methanosarcina thermophila soaked with coenzyme a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2AF3
- Type
- protein
- Length
- 664 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphate acetyltransferase
- EC
- 2.3.1.8
- UniProt
- P38503
- Ligands
- COA, SO4
- Pockets
- 6 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, D | Phosphate acetyltransferase (EC 2.3.1.8) | protein | 332 | 46% helix, 17% strand | P38503 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 515 | 0.70 | 0.80 | 51 | empty |
| 2 | 393 | 0.60 | 0.76 | 44 | COA |
| 3 | 228 | 0.57 | 0.79 | 27 | empty |
| 4 | 227 | 0.57 | 0.78 | 25 | empty |
| 5 | 217 | 0.56 | 0.79 | 36 | empty |
Interfaces
1 interface between chains.
- C–D · 1722 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 2AF3 · Phosphotransacetylase from Methanosarcina thermophila soaked with Coenzyme A · the same entry in another collection · chain C against C, TM-score 1.00
- P38503 · AlphaFold monomer V2.0 prediction for phosphate acetyltransferase (P38503) · a predicted model of the same protein · chain C against A, TM-score 0.91
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 P38503
- Elsewhere: RCSB PDB 2AF3 · PDBe 2AF3 · UniProt P38503
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