4ANB: PDB entry 4ANB

Crystal structures of human MEK1 with carboxamide-based allosteric inhibitor XL518 (GDC-0973), or related analogs. Determined by X-ray diffraction at 2.2 Å resolution. Released 19 Dec 2012.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: HOMO SAPIENS
Chains: 1
Atoms: 2,324
Mol. weight: 34.62 kDa
Ligands: MG, ACP, YQY
Released: 19 Dec 2012

Explore 4ANB in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4ANB contains 17 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: 17 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
α-helix	127-128	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	213-220	8
α-helix	227-229	3
α-helix	232-235	4
α-helix	242-258	17
α-helix	310-319	10
α-helix	321-323	3
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	301	HOMO SAPIENS	Q02750 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4ANB_1 DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE 1 (chains A)
MALGELKDDDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQIIRELQV
LHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGL
TYLREKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDEMANEFVGTRSYMSPERLQG
THYSVQSDIWSMGLSLVEMAVGRYPRPPMAIFELLDYIVNEPPPKLPSAVFSLEFQDFVN
KCLIKNPAERADLKQLMVHAFIKRSDAEEVDFAGWLCSTIGLNQPSTPTHAAGEGHHHHH
H

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	1
ACP	Phosphomethylphosphonic acid adenylate ester	C11 H18 N5 O12 P3	1
YQY	[3-(aminomethyl)-3-oxidanyl-azetidin-1-yl]-[3,4-bis(fluoranyl)-2-[(2-fluoranyl-…	C17 H15 F3 I N3 O2	1

Primary citation

Novel Carboxamide-Based Allosteric Mek Inhibitors: Discovery and Optimization Efforts Toward Xl518 (Gdc-0973). Rice, K.D., Aay, N., Anand, N.K. et al. ACS Med Chem Lett (2012) 3:416. DOI 10.1021/ML300049D · 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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