Research workbench
Human VH1-related dual-specificity phosphatase C124S mutant-peptide complex
Analyse Human VH1-related dual-specificity phosphatase C124S mutant-peptide complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1J4X
- Type
- protein
- Length
- 189 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dual specificity protein phosphatase 3; DDE(AHP)(TPO)G(PTR)VATR
- EC
- 3.1.3.48
- UniProt
- P51452
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual specificity protein phosphatase 3 (EC 3.1.3.48) | protein | 178 | 44% helix, 14% strand | P51452 |
| D | DDE(AHP)(TPO)G(PTR)VATR | protein | 11 | 0% helix, 0% strand | — |
Interfaces
1 interface between chains.
- A–D · 662 Ų buried · 28 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (phosphorylation, nonstandard).
Compared structures
- 1J4X · Human VH1-related dual-specificity phosphatase C124S mutant-peptide complex · the same entry in another collection · chain D against D, TM-score 1.00
- P51452 · AlphaFold monomer V2.0 prediction for dual specificity protein phosphatase 3 (P51452) · 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 P51452
- Elsewhere: RCSB PDB 1J4X · PDBe 1J4X · UniProt P51452
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