MolNFT v1 · #60851 · protein
Crystal structure of heptp in complex with a dually phosphorylated ERK2 peptide mimetic
3D44 · Tyrosine-protein phosphatase non-receptor type 7: “Crystal structure of heptp in complex with a dually phosphorylated ERK2 peptide mimetic”. X-ray diffraction, 1 ligand (CL), 2 pockets (best druggability 0.39). MolNFT v1 #60851 on…
- PDB
- 3D44
- Type
- protein
- Length
- 288 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein phosphatase non-receptor type 7; Mitogen-activated protein kinase 1…
- EC
- 3.1.3.48
- UniProt
- P35236, P28482
- Ligands
- CL
- Pockets
- 2 · best druggability 0.39
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein phosphatase non-receptor type 7 (EC 3.1.3.48) | protein | 284 | 39% helix, 23% strand | P35236 |
| B | Mitogen-activated protein kinase 1 peptide | protein | 4 | 0% helix, 0% strand | P28482 |
Ligands and binding sites
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 | 85 | 0.39 | 0.77 | 22 | empty |
| 2 | 51 | 0.24 | 0.73 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 397 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 3D44 · Crystal structure of HePTP in complex with a dually phosphorylated Erk2 peptide mimetic · the same entry in another collection · chain A against A, TM-score 1.00
- P35236 · AlphaFold monomer V2.0 prediction for tyrosine-protein phosphatase non-receptor type 7… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P35236
- Every structure of UniProt P28482
- Elsewhere: RCSB PDB 3D44 · PDBe 3D44 · UniProt P35236 · UniProt P28482
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.