MolNFT v1 · #2306 · protein
Cobalt deformylase inhibitor complex from E.COLI
1BSJ · Protein (peptide deformylase): “Cobalt deformylase inhibitor complex from E.COLI”. X-ray diffraction, 3 ligands (MLN, CO, PO4), 1 pocket (best druggability 0.51). MolNFT v1 #2306 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 1BSJ
- Type
- protein
- Length
- 166 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (peptide deformylase)
- EC
- 3.5.1.27
- UniProt
- P0A6K3
- Ligands
- MLN, CO, PO4
- Pockets
- 1 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (peptide deformylase) (EC 3.5.1.27) | protein | 166 | 36% helix, 27% strand | P0A6K3 |
Ligands and binding sites
- MLN · (S)-2-(phosphonoxy)caproyl-L-leucyl-P-nitroanilide · ligand · chains A
- CO · Cobalt (II) ion · metal · chains A
- PO4 · Phosphate ion · ion · chains A
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 | 140 | 0.51 | 0.80 | 23 | CO, MLN |
Compared structures
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 P0A6K3
- Elsewhere: RCSB PDB 1BSJ · PDBe 1BSJ · UniProt P0A6K3
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