MolNFT v1 · #127502 · protein
Convergent evolution involving dimeric and trimeric dutpases in signalling.
5MYF · Dutpase from di S. aureus phage: “Convergent evolution involving dimeric and trimeric dutpases in signalling.”. X-ray diffraction, 3 pockets (best druggability 0.49). MolNFT v1 #127502 on GenesisL1: 3D structure, binding sites and…
- PDB
- 5MYF
- Type
- protein
- Length
- 313 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dutpase from di S. aureus phage
- EC
- 3.6.1.23
- Pockets
- 3 · best druggability 0.49
Structure
x-ray diffraction · 2 distinct chains · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D | Dutpase from di S. aureus phage (EC 3.6.1.23) | protein | 158 | 72% helix, 0% strand | — |
| A | Dutpase from di S. aureus phage (EC 3.6.1.23) | protein | 155 | 71% helix, 0% strand | — |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 113 | 0.49 | 0.80 | 21 | empty |
| 2 | 93 | 0.41 | 0.77 | 21 | empty |
| 3 | 54 | 0.26 | 0.73 | 13 | empty |
Interfaces
1 interface between chains.
- D–A · 1329 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 5MYF · Convergent evolution involving dimeric and trimeric dUTPases in signalling. · the same entry in another collection · chain D against D, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 5MYF · PDBe 5MYF
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