MolNFT v1 · #47224 · protein
Structures of actinonin bound peptide deformylases from E. faecalis and S. pyogenes
2OS3: “Structures of actinonin bound peptide deformylases from E. faecalis and S. pyogenes”. X-ray diffraction, 2 ligands (BB2, CO), 1 pocket (best druggability 0.54). MolNFT v1 #47224 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 2OS3
- Type
- protein
- Length
- 205 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptide deformylase
- EC
- 3.5.1.88
- UniProt
- P68771
- Ligands
- BB2, CO
- Pockets
- 1 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptide deformylase (EC 3.5.1.88) | protein | 205 | 28% helix, 24% strand | P68771 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 183 | 0.54 | 0.79 | 26 | BB2 |
Compared structures
- 2OS3 · Structures of actinonin bound peptide deformylases from E. faecalis and S. pyogenes · the same entry in another collection · chain A against A, TM-score 1.00
- P68771 · AlphaFold monomer V2.0 prediction for peptide deformylase (P68771) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P68771
- Elsewhere: RCSB PDB 2OS3 · PDBe 2OS3 · UniProt P68771
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