GL1X · GenesisL1 explorer

Research workbench

Crystal structure of the MAP kinase binding domain of MKP5

Analyse Crystal structure of the MAP kinase binding domain of MKP5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2OUC
Type
protein
Length
264 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Dual specificity protein phosphatase 10
EC
3.1.3.48, 3.1.3.16
UniProt
Q9Y6W6

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BDual specificity protein phosphatase 10 (EC 3.1.3.48, 3.1.3.16)protein13244% helix, 16% strandQ9Y6W6

Interfaces

1 interface between chains.

  • A–B · 376 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 2OUC · Crystal structure of the MAP kinase binding domain of MKP5 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9Y6W6 · AlphaFold monomer V2.0 prediction for dual specificity protein phosphatase 10 (Q9Y6W6) · a predicted model of the same protein · chain A against A, TM-score 0.96

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.