MolNFT v1 · #120561 · protein
Crystal structure of the C-terminal lon protease-like domain of thermus thermophilus RADA/SMS
5H45 · DNA repair protein rada: “Crystal structure of the C-terminal lon protease-like domain of thermus thermophilus RADA/SMS”. X-ray diffraction, 1 pocket (best druggability 0.44). MolNFT v1 #120561 on GenesisL1: 3D structure, binding…
- PDB
- 5H45
- Type
- protein
- Length
- 309 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA repair protein rada
- UniProt
- Q5SKV2
- Pockets
- 1 · best druggability 0.44
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA repair protein rada | protein | 152 | 31% helix, 30% strand | Q5SKV2 |
| B | DNA repair protein rada | protein | 157 | 31% helix, 28% strand | Q5SKV2 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 88 | 0.44 | 0.79 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 799 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 5H45 · Crystal structure of the C-terminal Lon protease-like domain of Thermus thermophilus… · the same entry in another collection · chain A against A, 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
- Every structure of UniProt Q5SKV2
- Elsewhere: RCSB PDB 5H45 · PDBe 5H45 · UniProt Q5SKV2
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