MolNFT v1 · #66329 · protein
Crystal structure of the NK2 fragment (28-289) of human hepatocyte growth FACTOR/SCATTER factor
3HN4: “Crystal structure of the NK2 fragment (28-289) of human hepatocyte growth FACTOR/SCATTER factor”. X-ray diffraction, 1 ligand (SO4), 4 pockets (best druggability 0.48). MolNFT v1 #66329 on GenesisL1: 3D structure, binding sites and…
- PDB
- 3HN4
- Type
- protein
- Length
- 256 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hepatocyte growth factor
- UniProt
- P14210
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hepatocyte growth factor | protein | 256 | 6% helix, 26% strand | P14210 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 2 copies · chains A
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 158 | 0.48 | 0.77 | 24 | SO4 |
| 2 | 70 | 0.46 | 0.83 | 17 | empty |
| 3 | 107 | 0.40 | 0.76 | 16 | empty |
| 4 | 107 | 0.39 | 0.75 | 20 | empty |
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 3HN4 · Crystal structure of the NK2 fragment (28-289) of human hepatocyte growth factor/scatter… · the same entry in another collection · chain A against A, TM-score 1.00
- P14210 · AlphaFold monomer V2.0 prediction for hepatocyte growth factor (P14210) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 P14210
- Elsewhere: RCSB PDB 3HN4 · PDBe 3HN4 · UniProt P14210
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