3W8Q: Human Mitogen-Activated Protein Kinase Kinase 1

Structure of the Human Mitogen-Activated Protein Kinase Kinase 1 (MEK1). Determined by X-ray diffraction at 2.2 Å resolution. Released 26 Mar 2014.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,582
Mol. weight: 39.76 kDa
Ligands: AGS
Released: 26 Mar 2014

Explore 3W8Q in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3W8Q contains 21 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: 21 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	42-43	2
α-helix	44-58	15
α-helix	65-67	3
β-strand	68-76	9	1
β-strand	80-87	8	1
β-strand	93-100	8	1
α-helix	105-107	3
α-helix	108-119	12
β-strand	126	1	2
β-strand	129-134	6	1
β-strand	138-144	7	1
α-helix	145-146	2
β-strand	150	1	2
α-helix	151-158	8
α-helix	163-183	21
α-helix	193-195	3
β-strand	196-198	3	2
β-strand	204-206	3	2
α-helix	211-220	10
α-helix	232-235	4
α-helix	242-258	17
α-helix	265-267	3
α-helix	268-275	8
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	350	Homo sapiens	Q02750 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3W8Q_1 Dual specificity mitogen-activated protein kinase kinase 1 (chains A)
ELELDEQQRKRLEAFLTQKQKVGELKDDDFEKISELGAGNGGVVFKVSHKPSGLVMARKL
IHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKKA
GRIPEQILGKVSIAVIKGLTYLREKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDS
MANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIPPPDAKELELMFGCQ
VEGDAAETPPRPRAPGRPLASYGMDSRPPMAIFELLDYIVNEPPPKLPSGVFSLEFQDFV
NKCLIKNPAERADLKQLMVHAFIKRSDAEEVDFAGWLCSTIGLNHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
AGS	Phosphothiophosphoric acid-adenylate ester	C10 H16 N5 O12 P3 S	1

Primary citation

Structure of mitogen-activated protein kinase kinase 1 in the DFG-out conformation. Nakae, S., Kitamura, M., Fujiwara, D. et al. Acta Crystallogr F Struct Biol Commun (2021) 77:459-464. DOI 10.1107/S2053230X21011687 · 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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