3DV3: MEK1 with PF-04622664 Bound

MEK1 with PF-04622664 Bound. Determined by X-ray diffraction at 2.3 Å resolution. Released 21 Jul 2009.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,428
Mol. weight: 36.96 kDa
Ligands: MG, ATP, MEK
Released: 21 Jul 2009

Explore 3DV3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3DV3 contains 18 α-helices and 9 β-strands across 1 chain. 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 A: 18 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	65-67	3
β-strand	68-76	9	1
β-strand	80-87	8	1
β-strand	92-100	9	1
α-helix	105-115	11
α-helix	116-120	5
β-strand	126	1	2
β-strand	129-135	7	1
β-strand	138-144	7	1
β-strand	150	1	2
α-helix	151-158	8
α-helix	163-184	22
α-helix	193-195	3
β-strand	196-198	3	2
β-strand	204-206	3	2
α-helix	213-219	7
α-helix	232-236	5
α-helix	242-258	17
α-helix	265-267	3
α-helix	268-274	7
α-helix	310-319	10
α-helix	321-323	3
α-helix	325-326	2
α-helix	332-341	10
α-helix	352-356	5
α-helix	359-366	8
α-helix	371-379	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Dual specificity mitogen-activated protein kinase kinase 1	A	protein	322	Homo sapiens	Q02750 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3DV3_1 Dual specificity mitogen-activated protein kinase kinase 1 (chains A)
MELKDDDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQIIRELQVLHE
CNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYL
REKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFVGTRSYMSPERLQGTHY
SVQSDIWSMGLSLVEMAVGRYPIPPPDAKELELMFGCQVEGDAAETPPRPRTPGRPLSSY
GMDSRPPMAIFELLDYIVNEPPPKLPSGVFSLEFQDFVNKCLIKNPAERADLKQLMVHAF
IKRSDAEEVDFAGWLCSTIGLN

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	1
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	1
MEK	3,4-difluoro-2-[(2-fluoro-4-iodophenyl)amino]-N-(2-hydroxyethoxy)-5-[(2-hydroxy…	C18 H18 F3 I N2 O5	1

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

Primary citation

Beyond the MEK-pocket: can current MEK kinase inhibitors be utilized to synthesize novel type III NCKIs? Does the MEK-pocket exist in kinases other than MEK? Tecle, H., Shao, J., Li, Y. et al. Bioorg Med Chem Lett (2009) 19:226-229. DOI 10.1016/j.bmcl.2008.10.108 · PubMed

Other PDB entries of the same protein (UniProt Q02750 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7B7R 1.7 Å, MEK1 in complex with compound 4
7B9L 1.7 Å, MEK1 in complex with compound 23
3EQC 1.8 Å, X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a…
3EQI 1.9 Å, X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a…
3EQH 2.0 Å, X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a…
3VVH 2.0 Å, X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in complex…
7B94 2.0 Å, MEK1 in complex with compound 6
7F2X 2.01 Å, Crystal structure of MEK1 C121S mutant
9AXX 2.07 Å, Crystal structure of BRAF/MEK1 complex with NST-628 and an active RAF dimer
3EQD 2.1 Å, X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a…
4AN3 2.1 Å, Crystal structures of human MEK1 with carboxamide-based allosteric inhibitor XL518…
7XLP 2.1 Å, MEK1 bound to DS03090629

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