Research workbench
Crystal structure of PSY3-CSM2 complex
Analyse Crystal structure of PSY3-CSM2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VU9
- Type
- protein
- Length
- 406 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Platinum sensitivity protein 3; Chromosome segregation in meiosis protein 2
- UniProt
- Q12318, P40465
- Pockets
- 5 · best druggability 0.51
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Platinum sensitivity protein 3 | protein | 215 | 34% helix, 20% strand | Q12318 |
| B | Chromosome segregation in meiosis protein 2 | protein | 191 | 50% helix, 20% strand | P40465 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 2 copies · chains 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 149 | 0.51 | 0.79 | 23 | empty |
| 2 | 139 | 0.43 | 0.76 | 20 | empty |
| 3 | 112 | 0.42 | 0.77 | 17 | empty |
| 4 | 127 | 0.36 | 0.73 | 22 | empty |
| 5 | 58 | 0.32 | 0.76 | 15 | EDO |
Interfaces
1 interface between chains.
- A–B · 1238 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 3VU9 · Crystal Structure of Psy3-Csm2 complex · 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 B 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 A against A, TM-score 0.89
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 Q12318
- Every structure of UniProt P40465
- Elsewhere: RCSB PDB 3VU9 · PDBe 3VU9 · UniProt Q12318 · UniProt P40465
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