Research workbench
Structures of actinonin bound peptide deformylases from E. faecalis and S. pyogenes
Analyse Structures of actinonin bound peptide deformylases from E. faecalis and S.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- 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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