5HD4: Mitogen-activated protein kinase 1

Dissecting Therapeutic Resistance to ERK Inhibition Rat Wild Type SCH772984 in complex with (3R)-1-(2-oxo-2-{4-[4-(pyrimidin-2-yl)phenyl]piperazin-1-yl}ethyl)-N-[3-(pyridin-4-yl)-2H-indazol-5-yl]pyrrolidine-3-carboxamide. Determined by X-ray diffraction at 1.45 Å resolution. Released 24 Feb 2016.

Method: X-ray diffraction
Resolution: 1.45 Å
Organism: Rattus norvegicus
Chains: 1
Atoms: 3,191
Mol. weight: 43.46 kDa
Ligands: 38Z
Released: 24 Feb 2016

Explore 5HD4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5HD4 contains 23 α-helices and 15 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: 23 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	10-11	2	1
β-strand	16-17	2	1
β-strand	23-32	10	2
β-strand	35-42	8	2
β-strand	47-54	8	2
α-helix	60-75	16
β-strand	81	1	3
β-strand	86-88	3	2
β-strand	99-104	6	2
β-strand	108-109	2	3
α-helix	110-116	7
α-helix	118-120	3
α-helix	121-140	20
β-strand	143-144	2	4
α-helix	150-152	3
β-strand	153-155	3	3
β-strand	161-163	3	3
β-strand	170-171	2	4
α-helix	174-176	3
β-strand	178	1	5
α-helix	189-191	3
α-helix	194-198	5
β-strand	200	1	5
α-helix	206-221	16
α-helix	231-242	12
α-helix	245-246	2
α-helix	247-251	5
α-helix	256-264	9
α-helix	266-267	2
α-helix	269-272	4
α-helix	273-276	4
α-helix	282-291	10
α-helix	300-301	2
α-helix	302-306	5
α-helix	309-311	3
α-helix	317-319	3
α-helix	338-348	11
α-helix	350-352	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mitogen-activated protein kinase 1	A	protein	365	Rattus norvegicus	P63086 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5HD4_1 Mitogen-activated protein kinase 1 (chains A)
AHHHHHHMAAAAAAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNLNKVRVAIKK
ISPFEHQTYCQRTLREIKILLRFRHENIIGINDIIRAPTIEQMKDVYIVQDLMETDLYKL
LKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVAD
PDHDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLD
QLNHILGILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLT
FNPHKRIEVEQALAHPYLEQYYDPSDEPIAEAPFKFDMELDDLPKEKLKELIFEETARFQ
PGYRS

Ligands and cofactors

ID	Name	Formula	Copies
38Z	(3R)-1-(2-oxo-2-{4-[4-(pyrimidin-2-yl)phenyl]piperazin-1-yl}ethyl)-N-[3-(pyridi…	C33 H33 N9 O2	1

Water and common crystallization additives (SO4, PG4, DMS) are not listed.

Primary citation

Dissecting Therapeutic Resistance to ERK Inhibition. Jha, S., Morris, E.J., Hruza, A. et al. Mol Cancer Ther (2016) 15:548-559. DOI 10.1158/1535-7163.MCT-15-0172 · PubMed

Other PDB entries of the same protein (UniProt P63086 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4S32 1.34 Å, Crystal structure of ERK2 AMP-PNP complex
4S31 1.45 Å, Crystal structure of mitogen-activated protein kinase 1 wtERK2 at 1.45A
6DCG 1.45 Å, Discovery of MK-8353: An Orally Bioavailable Dual Mechanism ERK Inhibitor for Oncology
3QYZ 1.46 Å, Crystal structure of ERK2 in complex with an inhibitor
4XP0 1.46 Å, Crystal structure of ERK2 in complex with an inhibitor
4S2Z 1.48 Å, ERK2 Intrinsically active mutant R65S
4S33 1.48 Å, ERK2 R65S mutant complexed with AMP-PNP
6FLE 1.48 Å, Crystal structure of ERK2 in complex with an adenosine derivative
3QYW 1.5 Å, Crystal structure of ERK2 in complex with an inhibitor
8QR7 1.51 Å, Crystal structure of ERK2 in complex with a covalently bound macrocyclic ligand
8QRB 1.51 Å, Crystal structure of ERK2 in complex with a covalently bound macrocyclic ligand
6FI3 1.52 Å, Crystal structure of ERK2 in complex with an adenosine derivative

Browse structure collections

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