MolNFT v1 · #147106 · protein
Structure of human JAK2 FERM/SH2 in complex with leptin receptor
6E2P · Tyrosine-protein kinase JAK2: “Structure of human JAK2 FERM/SH2 in complex with leptin receptor”. X-ray diffraction, 1 ligand (SO4), 13 pockets (best druggability 0.80). MolNFT v1 #147106 on GenesisL1: 3D structure, binding sites…
- PDB
- 6E2P
- Type
- protein
- Length
- 938 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein kinase JAK2; Leptin receptor
- EC
- 2.7.10.2
- UniProt
- O60674, P48357
- Ligands
- SO4
- Pockets
- 13 · best druggability 0.80
Structure
x-ray diffraction · 4 distinct chains · 34% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein kinase JAK2 (EC 2.7.10.2) | protein | 457 | 34% helix, 26% strand | O60674 |
| B | Tyrosine-protein kinase JAK2 (EC 2.7.10.2) | protein | 443 | 34% helix, 24% strand | O60674 |
| C | Leptin receptor | protein | 20 | 15% helix, 0% strand | P48357 |
| D | Leptin receptor | protein | 18 | 33% helix, 0% strand | P48357 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 388 | 0.80 | 0.89 | 51 | empty |
| 2 | 378 | 0.78 | 0.88 | 51 | empty |
| 3 | 501 | 0.69 | 0.79 | 50 | empty |
| 4 | 330 | 0.59 | 0.77 | 32 | empty |
| 5 | 200 | 0.52 | 0.77 | 31 | empty |
Interfaces
3 interfaces between chains.
- A–C · 873 Ų buried · 12 hydrogen bonds · protein-protein
- B–D · 820 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 520 Ų buried · 10 hydrogen bonds · protein-protein
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 O60674
- Every structure of UniProt P48357
- Elsewhere: RCSB PDB 6E2P · PDBe 6E2P · UniProt O60674 · UniProt P48357
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