2Y4I: KSR2-MEK1 heterodimer

KSR2-MEK1 heterodimer. Determined by X-ray diffraction at 3.46 Å resolution. Released 19 Jan 2011.

Method
X-ray diffraction
Resolution
3.46 Å
Organisms
HOMO SAPIENS, ORYCTOLAGUS CUNICULUS
Chains
2
Atoms
4,661
Mol. weight
81.55 kDa
Ligands
ATP, MG
Released
19 Jan 2011

Explore 2Y4I in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2Y4I contains 34 α-helices and 29 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain B: 15 helices, 14 β-strands

ElementResiduesLengthSheet
α-helix656-6583
β-strand666-66721
β-strand67112
β-strand679-68352
β-strand684-68521
β-strand689-69352
α-helix696-6972
α-helix704-7085
α-helix711-7144
β-strand72213
β-strand727-73042
β-strand735-73842
β-strand74012
α-helix741-7422
β-strand745-74623
α-helix747-7504
α-helix761-77919
β-strand792-79433
β-strand800-80123
β-strand82314
α-helix827-8304
α-helix834-8374
β-strand84015
α-helix853-86917
α-helix879-8879
α-helix891-8933
α-helix903-9119
α-helix919-9202
α-helix921-9288
Chain C: 19 helices, 15 β-strands
ElementResiduesLengthSheet
α-helix44-5512
β-strand68-6926
β-strand73-7537
β-strand82-8327
β-strand86-8726
β-strand9216
β-strand95-10067
α-helix105-11511
α-helix116-1205
β-strand12318
β-strand12618
β-strand129-13357
β-strand138-14367
β-strand15018
α-helix151-1566
α-helix163-18422
α-helix193-1953
β-strand196-19838
β-strand204-20638
α-helix213-2186
β-strand22314
α-helix232-2365
α-helix242-25817
α-helix265-2662
α-helix271-2733
β-strand30915
α-helix310-31910
α-helix321-3233
α-helix325-3262
α-helix332-34110
α-helix350-3512
α-helix352-3565
α-helix359-3668
α-helix371-3755

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Kinase suppressor of ras 2Bprotein319HOMO SAPIENSQ6VAB6 (AlphaFold model)
Dual specificity mitogen-activated protein kinase kinase 1Cprotein395ORYCTOLAGUS CUNICULUSP29678 (AlphaFold model)
Sequence of entity 1 (B), FASTA
>2Y4I_1 KINASE SUPPRESSOR OF RAS 2 (chains B)
GPEMNLSLLSARSFPRKASQTSIFLQEWDIPFEQLEIGELIGKGRFGQVYHGRWHGEVAI
RLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLYSVV
RDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVVITDFGLFSISG
VLQAGRREDKLRIQNGWLCHLAPEIIRQLSPDTEEDKLPFSKHSDVFALGTIWYELHARE
WPFKTQPAEAIIWQMGTGMKPNLSQIGMGKEISDILLFCWAFEQEERPTFTKLMDMLEKL
PKRNRRLSHPGHFWKSAEL
Sequence of entity 2 (C), FASTA
>2Y4I_2 DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE 1 (chains C)
GPMPKKKPTPIQLNPAPDGSAVNGTSSAETNLEALQKKLLELELDEQQRKRLEAFLTQKQ
KVGELKDDDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQIIRELQVL
HECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLT
YLREKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFVGTRSYMSPERLQGT
HYSVQSDIWSMGLSLVEMAVGRYPIPPPDAKELELMFGCQVEGDAAETPPRPRTPGRPLS
SYGMDSRPPMAIFELLDYIVNEPPPKLPSAVFSLEFQDFVNKCLIKNPAERADLKQLMVH
AFIKRSDAEEVDFAGWLCSTIGLNQPSTPTHAAGV

Ligands and cofactors

IDNameFormulaCopies
ATPAdenosine-5'-triphosphateC10 H16 N5 O13 P32
MGMagnesium ionMg2

Water and common crystallization additives (CL) are not listed.

Primary citation

A Raf-Induced Allosteric Transition of Ksr Stimulates Ksr and Raf Phosphorylation of Mek. Brennan, D.F., Dar, A.C., Hertz, N.T. et al. Nature (2011) 472:366. DOI 10.1038/NATURE09860 · PubMed

Other PDB entries of the same protein (UniProt Q6VAB6 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 2Y4I directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.