Research workbench
Crystal structure of heptp in complex with a monophosphorylated ERK2 peptide
Analyse Crystal structure of heptp in complex with a monophosphorylated ERK2 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3D42
- Type
- protein
- Length
- 293 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
- Pockets
- 3 · best druggability 0.47
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein phosphatase non-receptor type 7 (EC 3.1.3.48) | protein | 289 | 38% 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
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 75 | 0.47 | 0.83 | 21 | GOL |
| 2 | 141 | 0.40 | 0.74 | 28 | empty |
| 3 | 58 | 0.28 | 0.74 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 372 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 3D42 · Crystal structure of HePTP in complex with a monophosphorylated Erk2 peptide · 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 0.98
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 3D42 · PDBe 3D42 · UniProt P35236 · UniProt P28482
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