MolNFT v1 · #17220 · protein
Crystal structure of PRFA,THE transcriptional regulator in listeria monocytogenes
1OMI · Listeriolysin regulatory protein: “Crystal structure of PRFA,THE transcriptional regulator in listeria monocytogenes”. X-ray diffraction, 4 pockets (best druggability 0.85). MolNFT v1 #17220 on GenesisL1: 3D structure, binding sites…
- PDB
- 1OMI
- Type
- protein
- Length
- 451 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Listeriolysin regulatory protein
- UniProt
- P22262
- Pockets
- 4 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Listeriolysin regulatory protein | protein | 224 | 44% helix, 25% strand | P22262 |
| B | Listeriolysin regulatory protein | protein | 227 | 46% helix, 26% strand | P22262 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1142 | 0.85 | 0.85 | 102 | empty |
| 2 | 50 | 0.71 | 0.98 | 15 | empty |
| 3 | 109 | 0.38 | 0.74 | 19 | empty |
| 4 | 108 | 0.35 | 0.73 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 2187 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 1OMI · Crystal structure of PrfA,the transcriptional regulator in Listeria monocytogenes · the same entry in another collection · chain A against A, TM-score 1.00
- P22262 · AlphaFold monomer V2.0 prediction for listeriolysin regulatory protein (P22262) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 P22262
- Elsewhere: RCSB PDB 1OMI · PDBe 1OMI · UniProt P22262
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