Research workbench
Structure of the 14-3-3/PMA2 complex stabilized by PYRROLIDONE1
Analyse Structure of the 14-3-3/PMA2 complex stabilized by PYRROLIDONE1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3M51
- Type
- protein
- Length
- 250 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3-like protein C; N.PLUMBAGINIFOLIA H+-translocating ATPase mRNA
- UniProt
- P93343, Q42932
- Ligands
- YR1
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3-like protein C | protein | 219 | 84% helix, 0% strand | P93343 |
| P | N.PLUMBAGINIFOLIA H+-translocating ATPase mRNA | protein | 31 | 35% helix, 0% strand | Q42932 |
Ligands and binding sites
- YR1 · 2-hydroxy-5-[(5S)-3-hydroxy-5-(4-nitrophenyl)-2-oxo-4-(phenylcarbonyl)-2,5-dihydro-1H-pyrrol-1-yl]benzoic acid · ligand · chains A, P
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 397 | 0.68 | 0.81 | 35 | YR1 |
| 2 | 150 | 0.46 | 0.77 | 17 | empty |
Interfaces
1 interface between chains.
- A–P · 1039 Ų buried · 12 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 P93343
- Every structure of UniProt Q42932
- Elsewhere: RCSB PDB 3M51 · PDBe 3M51 · UniProt P93343 · UniProt Q42932
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