Research workbench
Arbitrium peptide receptor from spbeta phage
Analyse Arbitrium peptide receptor from spbeta phage in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HP3
- Type
- protein
- Length
- 3,088 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SPBC2 prophage-derived uncharacterized protein yopk
- UniProt
- O31927
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | SPBC2 prophage-derived uncharacterized protein yopk | protein | 386 | 72% helix, 0% strand | O31927 |
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 480 | 0.84 | 0.91 | 38 | empty |
| 2 | 786 | 0.81 | 0.84 | 49 | empty |
| 3 | 639 | 0.80 | 0.85 | 43 | empty |
| 4 | 921 | 0.79 | 0.81 | 93 | empty |
| 5 | 744 | 0.78 | 0.82 | 47 | empty |
Interfaces
9 interfaces between chains.
- A–B · 1446 Ų buried · 16 hydrogen bonds · protein-protein
- E–F · 1294 Ų buried · 5 hydrogen bonds · protein-protein
- C–D · 1243 Ų buried · 15 hydrogen bonds · protein-protein
- G–H · 1174 Ų buried · 9 hydrogen bonds · protein-protein
- A–D · 698 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 120 modified (engineered).
Compared structures
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 O31927
- Elsewhere: RCSB PDB 6HP3 · PDBe 6HP3 · UniProt O31927
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