MolNFT v1 · #31063 · protein
S.PNEUMONIAE polypeptide deformylase complexed with sb- 505684
2AIE: “S.PNEUMONIAE polypeptide deformylase complexed with sb- 505684”. X-ray diffraction, 3 ligands (SB9, NI, SO4), 1 pocket (best druggability 0.50). MolNFT v1 #31063 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2AIE
- Type
- protein
- Length
- 194 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptide deformylase
- EC
- 3.5.1.88
- UniProt
- Q8DP79
- Ligands
- SB9, NI, SO4
- Pockets
- 1 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| P | Peptide deformylase (EC 3.5.1.88) | protein | 194 | 29% helix, 26% strand | Q8DP79 |
Ligands and binding sites
- SB9 · Hydroxy[3-(6-methylpyridin-2-yl)propyl]formamide · ligand · chains P
- NI · Nickel (II) ion · metal · chains P
- SO4 · Sulfate ion · ion · chains P
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 | 139 | 0.50 | 0.79 | 19 | SB9 |
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 Q8DP79
- Elsewhere: RCSB PDB 2AIE · PDBe 2AIE · UniProt Q8DP79
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.