MolNFT v1 · #86087 · protein
Hepatocyte growth factor-regulated tyrosine kinase substrate (hgs-hrs) bound to an IP2 compound at 1.68 a resolution
4AVX: “Hepatocyte growth factor-regulated tyrosine kinase substrate (hgs-hrs) bound to an IP2 compound at 1.68 a…”. X-ray diffraction, 2 ligands (ITP, ZN), 1 pocket (best druggability 0.57). MolNFT v1 #86087 on GenesisL1: 3D structure…
- PDB
- 4AVX
- Type
- protein
- Length
- 218 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
- ITP, ZN
- Pockets
- 1 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 56% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hepatocyte growth factor-regulated tyrosine kinase substrate | protein | 218 | 56% helix, 9% strand | O14964 |
Ligands and binding sites
- ITP · Phosphoric acid mono-(2,3,4,6-tetrahydroxy-5-phosphonooxy-cyclohexyl) ester · ligand · chains A
- ZN · Zinc ion · metal · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · 8 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 193 | 0.57 | 0.80 | 34 | empty |
Compared structures
- 4AVX · Hepatocyte Growth Factor-Regulated Tyrosine Kinase Substrate (Hgs-Hrs) bound to an IP2… · 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 0.80
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 4AVX · PDBe 4AVX · UniProt O14964
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