MolNFT v1 · #18154 · protein
Methionyl-tRNA synthetase from escherichia COLI complexed with trifluoromethionine
1PFW: “Methionyl-tRNA synthetase from escherichia COLI complexed with trifluoromethionine”. X-ray diffraction, 2 ligands (MF3, ZN), 2 pockets (best druggability 0.64). MolNFT v1 #18154 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 1PFW
- Type
- protein
- Length
- 546 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methionyl-tRNA synthetase
- EC
- 6.1.1.10
- UniProt
- P00959
- Ligands
- MF3, ZN
- Pockets
- 2 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methionyl-tRNA synthetase (EC 6.1.1.10) | protein | 546 | 51% helix, 16% strand | P00959 |
Ligands and binding sites
- MF3 · 2-amino-4-trifluoromethylsulfanyl-butyric acid · ligand · chains A
- ZN · Zinc ion · metal · chains A
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 | 337 | 0.64 | 0.79 | 32 | MF3 |
| 2 | 246 | 0.56 | 0.77 | 42 | empty |
Compared structures
- 1PFW · Methionyl-tRNA synthetase from escherichia COLI complexed with trifluoromethionine · the same entry in another collection · chain A against A, TM-score 1.00
- P00959 · AlphaFold monomer V2.0 prediction for methionine--tRNA ligase (P00959) · 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 P00959
- Elsewhere: RCSB PDB 1PFW · PDBe 1PFW · UniProt P00959
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