MolNFT v1 · #190514 · protein
Crystal structure of human rptph
7XC0 · Receptor-type tyrosine-protein phosphatase H: “Crystal structure of human rptph”. X-ray diffraction, 1 ligand (PO4), 3 pockets (best druggability 0.36). MolNFT v1 #190514 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7XC0
- Type
- protein
- Length
- 287 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Receptor-type tyrosine-protein phosphatase H
- EC
- 3.1.3.48
- UniProt
- Q9HD43
- Ligands
- PO4
- Pockets
- 3 · best druggability 0.36
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receptor-type tyrosine-protein phosphatase H (EC 3.1.3.48) | protein | 287 | 38% helix, 21% strand | Q9HD43 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 77 | 0.36 | 0.77 | 18 | empty |
| 2 | 75 | 0.32 | 0.75 | 18 | empty |
| 3 | 51 | 0.28 | 0.75 | 11 | empty |
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 Q9HD43
- Elsewhere: RCSB PDB 7XC0 · PDBe 7XC0 · UniProt Q9HD43
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