MolNFT v1 · #15272 · protein
Crystal structure of pyruvate formate-lyase with pyruvate
1MZO: “Crystal structure of pyruvate formate-lyase with pyruvate”. X-ray diffraction, 1 ligand (PYR), 10 pockets (best druggability 0.87). MolNFT v1 #15272 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1MZO
- Type
- protein
- Length
- 1,512 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pyruvate formate-lyase
- EC
- 2.3.1.54
- UniProt
- P09373
- Ligands
- PYR
- Pockets
- 10 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Pyruvate formate-lyase (EC 2.3.1.54) | protein | 756 | 47% helix, 12% strand | P09373 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 749 | 0.87 | 0.90 | 65 | empty |
| 2 | 89 | 0.73 | 0.96 | 29 | empty |
| 3 | 83 | 0.73 | 0.96 | 29 | empty |
| 4 | 50 | 0.70 | 0.98 | 17 | empty |
| 5 | 124 | 0.41 | 0.75 | 28 | empty |
Interfaces
1 interface between chains.
- A–B · 2028 Ų buried · 30 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 1MZO · PDBe 1MZO · UniProt P09373
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