Research workbench
Human 14-3-3 sigma isoform in complex with plp
Analyse Human 14-3-3 sigma isoform in complex with plp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6TM7
- Type
- protein
- Length
- 447 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 14-3-3 protein sigma
- UniProt
- P31947
- Ligands
- PLP, SO4
- Pockets
- 4 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 14-3-3 protein sigma | protein | 224 | 78% helix, 0% strand | P31947 |
| B | 14-3-3 protein sigma | protein | 223 | 77% helix, 0% strand | P31947 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 500 | 0.61 | 0.75 | 35 | empty |
| 2 | 56 | 0.36 | 0.79 | 15 | empty |
| 3 | 72 | 0.35 | 0.76 | 16 | empty |
| 4 | 76 | 0.32 | 0.74 | 17 | PLP |
Interfaces
1 interface between chains.
- A–B · 260 Ų buried · 2 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 P31947
- Elsewhere: RCSB PDB 6TM7 · PDBe 6TM7 · UniProt P31947
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