Research workbench
The transcriptional regulator prfa-L140H mutant from listeria monocytogenes
Analyse The transcriptional regulator prfa-L140H mutant from listeria monocytogenes in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6QVZ
- Type
- protein
- Length
- 465 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Listeriolysin positive regulatory factor a
- UniProt
- Q4TVQ0
- Ligands
- NA
- Pockets
- 5 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Listeriolysin positive regulatory factor a | protein | 229 | 47% helix, 28% strand | Q4TVQ0 |
| B | Listeriolysin positive regulatory factor a | protein | 236 | 45% helix, 25% strand | Q4TVQ0 |
Ligands and binding sites
- NA · Sodium ion · metal · 3 copies · chains A, B
- IPA · Isopropyl alcohol · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 426 | 0.79 | 0.87 | 44 | IPA |
| 2 | 494 | 0.79 | 0.86 | 49 | IPA |
| 3 | 56 | 0.73 | 0.99 | 19 | IPA |
| 4 | 426 | 0.72 | 0.82 | 54 | empty |
| 5 | 51 | 0.24 | 0.73 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 2194 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 6QVZ · The Transcriptional Regulator PrfA-L140H mutant from Listeria Monocytogenes · the same entry in another collection · chain A against A, TM-score 1.00
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 Q4TVQ0
- Elsewhere: RCSB PDB 6QVZ · PDBe 6QVZ · UniProt Q4TVQ0
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