Research workbench
Crystal structure of the PSY3-CSM2 complex
Analyse Crystal structure of the 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
- 4DT1
- Type
- protein
- Length
- 404 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 · 43% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chromosome segregation in meiosis protein 2 | protein | 193 | 51% helix, 19% strand | P40465 |
| B | Platinum sensitivity protein 3 | protein | 211 | 35% helix, 19% strand | Q12318 |
Ligands and binding sites
- EOH · Ethanol · additive · 4 copies · chains A, 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 | 92 | 0.51 | 0.83 | 16 | empty |
| 2 | 100 | 0.33 | 0.73 | 26 | empty |
| 3 | 51 | 0.30 | 0.76 | 17 | empty |
| 4 | 73 | 0.29 | 0.73 | 18 | EOH |
| 5 | 56 | 0.29 | 0.75 | 14 | EOH |
Interfaces
1 interface between chains.
- A–B · 1184 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 4DT1 · Crystal structure of the 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 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 0.89
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 P40465
- Every structure of UniProt Q12318
- Elsewhere: RCSB PDB 4DT1 · PDBe 4DT1 · UniProt P40465 · UniProt Q12318
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