MolNFT v1 · #135531 · protein
Crystal structure of the saccharomyces cerevisiae separase-securin complex at 2.6 ångström resolution
5U1T · Separin: “Crystal structure of the saccharomyces cerevisiae separase-securin complex at 2.6 ångström resolution”. X-ray diffraction, 20 pockets (best druggability 0.87). MolNFT v1 #135531 on GenesisL1: 3D structure, binding sites…
- PDB
- 5U1T
- Type
- protein
- Length
- 1,552 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Separin; Securin
- EC
- 3.4.22.49
- UniProt
- Q03018, P40316
- Pockets
- 20 · best druggability 0.87
Structure
x-ray diffraction · 2 distinct chains · 62% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Separin (EC 3.4.22.49) | protein | 1486 | 63% helix, 5% strand | Q03018 |
| B | Securin | protein | 66 | 27% helix, 0% strand | P40316 |
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 728 | 0.87 | 0.90 | 60 | empty |
| 2 | 449 | 0.78 | 0.86 | 64 | empty |
| 3 | 133 | 0.69 | 0.90 | 16 | empty |
| 4 | 443 | 0.69 | 0.80 | 47 | empty |
| 5 | 81 | 0.59 | 0.88 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 4239 Ų buried · 50 hydrogen bonds · protein-protein
Compared structures
- 5U1T · Crystal structure of the Saccharomyces cerevisiae separase-securin complex at 2.6… · the same entry in another collection · chain A against A, TM-score 1.00
- Q03018 · AlphaFold monomer V2.0 prediction for separin (Q03018) · a predicted model of the same protein · chain A against A, TM-score 0.98
- P40316 · AlphaFold monomer V2.0 prediction for securin (P40316) · a predicted model of the same protein · chain B against A, TM-score 0.56
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 Q03018
- Every structure of UniProt P40316
- Elsewhere: RCSB PDB 5U1T · PDBe 5U1T · UniProt Q03018 · UniProt P40316
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