Current Protein Identity:A0A125YG37 New Search
Main Difference Dimensions in This Set
Different mutation/modification Different ligand/ion Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
9TYG Structure of the MAP2K MEK1 in an inactive conformation in complex with its substrate MAPK ERK2 Deposited 2026-01-19 Assembly 1 Insufficient information Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 441–455(15 aa)
Mutation:residue 3-11 replaced with 15 residues GRA24 KIM,Ser218Asp,Ser222Asp ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.90 Å
9TYH Structure of the MAP2K MEK1 in an active conformation in complex with its substrate MAPK ERK2 Deposited 2026-01-19 Assembly 1 Insufficient information Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 441–455(15 aa)
Mutation:residue 3-11 replaced with GRA24 KIM (15 residues),Ser218Asp,Ser222Asp ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
9TYI Structure of the MAP2K MEK1 without bound nucleotide in complex with its substrate MAPK ERK2 Deposited 2026-01-19 Assembly 1 Insufficient information Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 441–455(15 aa)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å