Research workbench
The crystal structure of PSY3-CSM2 complex from budding yeast
Analyse The crystal structure of PSY3-CSM2 complex from budding yeast in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EQ6
- Type
- protein
- Length
- 402 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chromosome segregation in meiosis protein 2; Platinum sensitivity protein 3
- UniProt
- P40465, Q12318
- Pockets
- 5 · best druggability 0.51
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chromosome segregation in meiosis protein 2 | protein | 192 | 52% helix, 19% strand | P40465 |
| B | Platinum sensitivity protein 3 | protein | 210 | 37% helix, 19% strand | Q12318 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 141 | 0.51 | 0.79 | 20 | empty |
| 2 | 108 | 0.36 | 0.74 | 19 | empty |
| 3 | 81 | 0.34 | 0.76 | 18 | empty |
| 4 | 50 | 0.31 | 0.77 | 14 | empty |
| 5 | 81 | 0.29 | 0.72 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1289 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 4EQ6 · The crystal structure of Psy3-Csm2 complex from budding yeast · the same entry in another collection · chain A against A, TM-score 1.00
- P40465 · AlphaFold monomer V2.0 prediction for chromosome segregation in meiosis protein 2 (P40465) · a predicted model of the same protein · chain A against A, TM-score 0.98
- Q12318 · AlphaFold monomer V2.0 prediction for platinum sensitivity protein 3 (Q12318) · a predicted model of the same protein · chain B against A, TM-score 0.88
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 P40465
- Every structure of UniProt Q12318
- Elsewhere: RCSB PDB 4EQ6 · PDBe 4EQ6 · UniProt P40465 · UniProt Q12318
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