Research workbench
Structure of human JAK2 FERM/SH2 in complex with erythropoietin receptor
Analyse Structure of human JAK2 FERM/SH2 in complex with erythropoietin receptor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6E2Q
- Type
- protein
- Length
- 2,037 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein kinase JAK2; Erythropoietin receptor
- EC
- 2.7.10.2
- UniProt
- O60674, P19235
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 8 distinct chains · 35% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein kinase JAK2 (EC 2.7.10.2) | protein | 473 | 35% helix, 27% strand | O60674 |
| B | Tyrosine-protein kinase JAK2 (EC 2.7.10.2) | protein | 470 | 34% helix, 27% strand | O60674 |
| C | Tyrosine-protein kinase JAK2 (EC 2.7.10.2) | protein | 463 | 36% helix, 26% strand | O60674 |
| D | Tyrosine-protein kinase JAK2 (EC 2.7.10.2) | protein | 431 | 37% helix, 25% strand | O60674 |
| M | Erythropoietin receptor | protein | 44 | 30% helix, 5% strand | P19235 |
| N | Erythropoietin receptor | protein | 57 | 25% helix, 7% strand | P19235 |
| O | Erythropoietin receptor | protein | 52 | 27% helix, 8% strand | P19235 |
| P | Erythropoietin receptor | protein | 47 | 28% helix, 4% strand | P19235 |
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 475 | 0.81 | 0.88 | 64 | empty |
| 2 | 409 | 0.80 | 0.89 | 53 | empty |
| 3 | 420 | 0.79 | 0.87 | 54 | empty |
| 4 | 394 | 0.78 | 0.87 | 48 | empty |
| 5 | 875 | 0.73 | 0.77 | 93 | empty |
Interfaces
16 interfaces between chains.
- A–N · 2083 Ų buried · 19 hydrogen bonds · protein-protein
- B–O · 2074 Ų buried · 17 hydrogen bonds · protein-protein
- C–M · 1448 Ų buried · 17 hydrogen bonds · protein-protein
- D–P · 1439 Ų buried · 12 hydrogen bonds · protein-protein
- B–P · 438 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 6E2Q · Structure of human JAK2 FERM/SH2 in complex with Erythropoietin Receptor · the same entry in another collection · chain P against P, TM-score 1.00
- P19235 · AlphaFold monomer V2.0 prediction for erythropoietin receptor (P19235) · a predicted model of the same protein · chain M against A, TM-score 0.45
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 P19235
- Elsewhere: RCSB PDB 6E2Q · PDBe 6E2Q · UniProt O60674 · UniProt P19235
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