Research workbench
Rhcc in complex with pyrene
Analyse Rhcc in complex with pyrene in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5VH0
- Type
- protein
- Length
- 194 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tetrabrachion
- UniProt
- Q54436
- Ligands
- 8P0
Structure
x-ray diffraction · 3 distinct chains · 93% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Tetrabrachion | protein | 49 | 94% helix, 0% strand | Q54436 |
| B | Tetrabrachion | protein | 48 | 94% helix, 0% strand | Q54436 |
| C | Tetrabrachion | protein | 48 | 92% helix, 0% strand | Q54436 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–B · 1053 Ų buried · 9 hydrogen bonds · protein-protein
- C–D · 1019 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 449 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 5VH0 · RHCC in complex with pyrene · 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 Q54436
- Elsewhere: RCSB PDB 5VH0 · PDBe 5VH0 · UniProt Q54436
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.