Research workbench
4FE-4S-pyruvate formate-lyase activating enzyme with partially disordered adomet
Analyse 4FE-4S-pyruvate formate-lyase activating enzyme with partially disordered adomet in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3C8F
- Type
- protein
- Length
- 245 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pyruvate formate-lyase 1-activating enzyme
- EC
- 1.97.1.4
- UniProt
- P0A9N4
- Ligands
- SF4, MT2
- Pockets
- 1 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pyruvate formate-lyase 1-activating enzyme (EC 1.97.1.4) | protein | 245 | 39% helix, 21% strand | P0A9N4 |
Ligands and binding sites
- SF4 · Iron/sulfur cluster · ligand · chains A
- MT2 · [(3S)-3-amino-3-carboxypropyl](ethyl)methylsulfonium · ligand · chains A
- PGE · Triethylene glycol · additive · 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 | 501 | 0.71 | 0.80 | 46 | SF4, MT2, PGE |
Compared structures
- 3C8F · 4Fe-4S-Pyruvate formate-lyase Activating Enzyme with partially disordered AdoMet · the same entry in another collection · chain A against A, TM-score 1.00
- P0A9N4 · AlphaFold monomer V2.0 prediction for pyruvate formate-lyase 1-activating enzyme (P0A9N4) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P0A9N4
- Elsewhere: RCSB PDB 3C8F · PDBe 3C8F · UniProt P0A9N4
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