MolNFT v1 · #84903 · protein
Crystal structure of the tandem vhs and fyve domains of hepatocyte growth factor-regulated tyrosine kinase substrate (hgs-hrs) at 1.48 a resolution
3ZYQ: “Crystal structure of the tandem vhs and fyve domains of hepatocyte growth factor-regulated tyrosine kinase…”. X-ray diffraction, 2 ligands (ZN, SO4), 2 pockets (best druggability 0.52). MolNFT v1 #84903 on GenesisL1: 3D structure…
- PDB
- 3ZYQ
- Type
- protein
- Length
- 216 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hepatocyte growth factor-regulated tyrosine kinase substrate
- UniProt
- O14964
- Ligands
- ZN, SO4
- Pockets
- 2 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hepatocyte growth factor-regulated tyrosine kinase substrate | protein | 216 | 55% helix, 9% strand | O14964 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
- SO4 · Sulfate ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 145 | 0.52 | 0.80 | 17 | empty |
| 2 | 84 | 0.38 | 0.77 | 18 | empty |
Compared structures
- 3ZYQ · Crystal structure of the tandem VHS and FYVE domains of Hepatocyte growth… · the same entry in another collection · chain A against A, TM-score 1.00
- O14964 · AlphaFold monomer V2.0 prediction for hepatocyte growth factor- regulated tyrosine kinase… · a predicted model of the same protein · chain A against A, TM-score 0.71
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 O14964
- Elsewhere: RCSB PDB 3ZYQ · PDBe 3ZYQ · UniProt O14964
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