MolNFT v1 · #68493 · protein
Ca-like domain of mouse ptprg
3JXG · Receptor-type tyrosine-protein phosphatase gamma: “Ca-like domain of mouse ptprg”. X-ray diffraction, 15 pockets (best druggability 0.72). MolNFT v1 #68493 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3JXG
- Type
- protein
- Length
- 1,039 residues
- Chains
- 4
- 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
- Q05909
- Pockets
- 15 · best druggability 0.72
Structure
x-ray diffraction · 4 distinct chains · 17% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receptor-type tyrosine-protein phosphatase gamma (EC 3.1.3.48) | protein | 257 | 18% helix, 30% strand | Q05909 |
| B | Receptor-type tyrosine-protein phosphatase gamma (EC 3.1.3.48) | protein | 259 | 18% helix, 31% strand | Q05909 |
| C | Receptor-type tyrosine-protein phosphatase gamma (EC 3.1.3.48) | protein | 264 | 17% helix, 32% strand | Q05909 |
| D | Receptor-type tyrosine-protein phosphatase gamma (EC 3.1.3.48) | protein | 259 | 18% helix, 32% strand | Q05909 |
Pockets
15 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 441 | 0.72 | 0.82 | 65 | empty |
| 2 | 172 | 0.64 | 0.85 | 27 | empty |
| 3 | 232 | 0.53 | 0.76 | 28 | empty |
| 4 | 110 | 0.50 | 0.81 | 22 | empty |
| 5 | 175 | 0.49 | 0.76 | 24 | empty |
Interfaces
5 interfaces between chains.
- B–D · 732 Ų buried · 15 hydrogen bonds · protein-protein
- B–C · 337 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 285 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 238 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 110 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 4 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 Q05909
- Elsewhere: RCSB PDB 3JXG · PDBe 3JXG · UniProt Q05909
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