Research workbench
Crystal structure of S. pombe MEI2 RRM3 domain
Analyse Crystal structure of S. pombe MEI2 RRM3 domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6YYL
- Type
- protein
- Length
- 293 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Meiosis protein MEI2
- UniProt
- P08965
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Meiosis protein MEI2 | protein | 147 | 29% helix, 24% strand | P08965 |
| C | Meiosis protein MEI2 | protein | 146 | 28% helix, 24% strand | P08965 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 7 copies · chains A, C
- EDO · 1,2-ethanediol · additive · 9 copies · chains A, C
- PEG · Di(hydroxyethyl)ether · additive · 3 copies · 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 | 569 | 0.69 | 0.78 | 67 | EDO, SO4 |
Interfaces
1 interface between chains.
- A–C · 552 Ų buried · 1 hydrogen bond · 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 P08965
- Elsewhere: RCSB PDB 6YYL · PDBe 6YYL · UniProt P08965
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.