Research workbench
Crystal structure of a singleton protein PF1176 from P. furiosus
Analyse Crystal structure of a singleton protein PF1176 from P. furiosus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HJM
- Type
- protein
- Length
- 362 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein PF1176
- UniProt
- Q8U1N0
- Pockets
- 5 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Hypothetical protein PF1176 | protein | 91 | 75% helix, 0% strand | Q8U1N0 |
| C, D | Hypothetical protein PF1176 | protein | 90 | 78% helix, 0% strand | Q8U1N0 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 62 | 0.56 | 0.89 | 15 | empty |
| 2 | 66 | 0.31 | 0.75 | 21 | empty |
| 3 | 54 | 0.28 | 0.75 | 15 | empty |
| 4 | 64 | 0.27 | 0.72 | 14 | empty |
| 5 | 52 | 0.23 | 0.71 | 13 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1166 Ų buried · 9 hydrogen bonds · protein-protein
- C–D · 1100 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 898 Ų buried · 16 hydrogen bonds · protein-protein
- A–D · 58 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 56 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 2HJM · Crystal structure of a singleton protein PF1176 from P. furiosus · 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 Q8U1N0
- Elsewhere: RCSB PDB 2HJM · PDBe 2HJM · UniProt Q8U1N0
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