Research workbench
Crystal structure of protein DR1152 from deinococcus radiodurans R1, pfam DUF861
Analyse Crystal structure of protein DR1152 from deinococcus radiodurans R1, pfam DUF861 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SFN
- Type
- protein
- Length
- 490 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Conserved hypothetical protein
- UniProt
- Q9RV77
- Pockets
- 4 · best druggability 0.47
Structure
x-ray diffraction · 1 distinct chain · 2% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Conserved hypothetical protein | protein | 245 | 2% helix, 50% strand | Q9RV77 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 99 | 0.47 | 0.80 | 20 | empty |
| 2 | 109 | 0.46 | 0.79 | 22 | empty |
| 3 | 85 | 0.33 | 0.74 | 22 | empty |
| 4 | 67 | 0.30 | 0.74 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 570 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 1SFN · Crystal structure of protein DR1152 from Deinococcus radiodurans R1, Pfam DUF861 · 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 Q9RV77
- Elsewhere: RCSB PDB 1SFN · PDBe 1SFN · UniProt Q9RV77
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