MolNFT v1 · #39830 · protein
Crystal structure of protein DR0370 from deinococcus radiodurans, pfam DUF178
2I6E · Hypothetical protein: “Crystal structure of protein DR0370 from deinococcus radiodurans, pfam DUF178”. X-ray diffraction, 1 ligand (SO4), 20 pockets (best druggability 0.87). MolNFT v1 #39830 on GenesisL1: 3D structure, binding…
- PDB
- 2I6E
- Type
- protein
- Length
- 2,176 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein
- UniProt
- Q9RXE3
- Ligands
- SO4
- Pockets
- 20 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Hypothetical protein | protein | 272 | 42% helix, 20% strand | Q9RXE3 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 18 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1145 | 0.87 | 0.88 | 115 | SO4 |
| 2 | 1200 | 0.86 | 0.87 | 117 | SO4 |
| 3 | 73 | 0.73 | 0.98 | 20 | empty |
| 4 | 68 | 0.73 | 0.99 | 17 | empty |
| 5 | 65 | 0.72 | 0.98 | 19 | empty |
Interfaces
6 interfaces between chains.
- E–F · 1575 Ų buried · 15 hydrogen bonds · protein-protein
- A–B · 1561 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 1558 Ų buried · 13 hydrogen bonds · protein-protein
- G–H · 1538 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 899 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 32 modified (engineered).
Compared structures
- 2I6E · Crystal structure of protein DR0370 from Deinococcus radiodurans, Pfam DUF178 · 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 Q9RXE3
- Elsewhere: RCSB PDB 2I6E · PDBe 2I6E · UniProt Q9RXE3
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