MolNFT v1 · #20526 · protein
Crystal structure of human TYRO3-D1D2
1RHF · Tyrosine-protein kinase receptor TYRO3: “Crystal structure of human TYRO3-D1D2”. X-ray diffraction, 1 ligand (ZN), 1 pocket (best druggability 0.32). MolNFT v1 #20526 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1RHF
- Type
- protein
- Length
- 352 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein kinase receptor TYRO3
- EC
- 2.7.1.112
- UniProt
- Q06418
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.32
Structure
x-ray diffraction · 1 distinct chain · 2% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Tyrosine-protein kinase receptor TYRO3 (EC 2.7.1.112) | protein | 176 | 2% helix, 57% strand | Q06418 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A, B
- ACT · Acetate ion · additive · 4 copies · chains A, B
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 72 | 0.32 | 0.74 | 21 | ACT |
Interfaces
1 interface between chains.
- A–B · 264 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide, 4 modified (disulfide, 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 Q06418
- Elsewhere: RCSB PDB 1RHF · PDBe 1RHF · UniProt Q06418
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.