Research workbench
Crystal structure of C418A,C419A mutant of pfl from E.COLI
Analyse Crystal structure of C418A,C419A mutant of pfl from E.COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CM5
- 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, CO3
- Pockets
- 10 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein (pyruvate formate-lyase) (EC 2.3.1.54) | protein | 759 | 47% helix, 13% 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 | 1119 | 0.84 | 0.85 | 116 | empty |
| 2 | 97 | 0.74 | 0.96 | 32 | empty |
| 3 | 104 | 0.72 | 0.94 | 31 | empty |
| 4 | 95 | 0.66 | 0.91 | 34 | empty |
| 5 | 71 | 0.39 | 0.79 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 2034 Ų buried · 27 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 1CM5 · PDBe 1CM5 · UniProt P09373
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