MolNFT v1 · #68494 · protein
Ca-like domain of human ptprg
3JXH · Receptor-type tyrosine-protein phosphatase gamma: “Ca-like domain of human ptprg”. X-ray diffraction, 1 ligand (SO4), 2 pockets (best druggability 0.46). MolNFT v1 #68494 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3JXH
- Type
- protein
- Length
- 257 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Receptor-type tyrosine-protein phosphatase gamma
- EC
- 3.1.3.48
- UniProt
- P23470
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 18% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | Receptor-type tyrosine-protein phosphatase gamma (EC 3.1.3.48) | protein | 257 | 18% helix, 30% strand | P23470 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 121 | 0.46 | 0.78 | 18 | empty |
| 2 | 94 | 0.40 | 0.77 | 19 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 P23470
- Elsewhere: RCSB PDB 3JXH · PDBe 3JXH · UniProt P23470
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