MolNFT v1 · #47994 · protein
Crystal structure of pfl from E.COLI
2PFL · Protein (pyruvate formate-lyase): “Crystal structure of pfl from E.COLI”. X-ray diffraction, 2 ligands (NA, CL), 11 pockets (best druggability 0.85). MolNFT v1 #47994 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2PFL
- Type
- protein
- Length
- 1,518 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (pyruvate formate-lyase)
- EC
- 2.3.1.54
- UniProt
- P09373
- Ligands
- NA, CL
- Pockets
- 11 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein (pyruvate formate-lyase) (EC 2.3.1.54) | protein | 759 | 47% helix, 11% strand | P09373 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1016 | 0.85 | 0.86 | 105 | empty |
| 2 | 105 | 0.76 | 0.97 | 32 | empty |
| 3 | 108 | 0.74 | 0.95 | 31 | empty |
| 4 | 130 | 0.62 | 0.86 | 38 | empty |
| 5 | 97 | 0.58 | 0.86 | 28 | empty |
Interfaces
1 interface between chains.
- A–B · 2022 Ų buried · 26 hydrogen bonds · protein-protein
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 P09373
- Elsewhere: RCSB PDB 2PFL · PDBe 2PFL · UniProt P09373
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.