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Crystal structure of the MEK1 fha domain in complex with the HOP1 PTHR318 peptide.

Analyse Crystal structure of the MEK1 fha domain in complex with the HOP1 PTHR318… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5YYZ
Type
protein
Length
109 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Meiosis-specific SERINE/THREONINE-protein kinase MEK1; Meiosis-specific protein HOP1
EC
2.7.11.1
UniProt
P24719, P20050

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 41% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMeiosis-specific SERINE/THREONINE-protein kinase MEK1 (EC 2.7.11.1)protein1020% helix, 44% strandP24719
BMeiosis-specific protein HOP1protein70% helix, 0% strandP20050

Interfaces

1 interface between chains.

  • A–B · 381 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

  • 5YYZ · Crystal structure of the MEK1 FHA domain in complex with the HOP1 pThr318 peptide. · the same entry in another collection · chain A against A, TM-score 1.00
  • P24719 · AlphaFold monomer V2.0 prediction for meiosis-specific SERINE/THREONINE-protein kinase… · a predicted model of the same protein · chain A against A, TM-score 0.97
  • P20050 · AlphaFold monomer V2.0 prediction for meiosis-specific protein HOP1 (P20050) · a predicted model of the same protein · chain B against A, TM-score 0.66

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