4S31: Mitogen-activated protein kinase 1 wtERK2

Crystal structure of mitogen-activated protein kinase 1 wtERK2 at 1.45A. Determined by X-ray diffraction at 1.45 Å resolution. Released 27 Jan 2016.

Method: X-ray diffraction
Resolution: 1.45 Å
Organism: Rattus norvegicus
Chains: 1
Atoms: 3,033
Mol. weight: 41.33 kDa
Released: 27 Jan 2016

Explore 4S31 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4S31 contains 24 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: 24 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	6	1	1
β-strand	16	1	1
β-strand	23-28	6	2
β-strand	35-42	8	2
β-strand	47-54	8	2
α-helix	60-75	16
β-strand	81	1	3
α-helix	82-84	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	194-197	4
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	358	Rattus norvegicus	P63086 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4S31_1 Mitogen-activated protein kinase 1 (chains A)
MAAAAAAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNLNKVRVAIKKISPFEHQ
TYCQRTLREIKILLRFRHENIIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKTQHLS
NDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADPDHDHTG
FLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILG
ILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRI
EVEQALAHPYLEQYYDPSDEPIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGYRS

Primary citation

Multiple mechanisms render Erk proteins MEK-independent. Livnah, O., Karamansha, Y. To be published.

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
5HD4 1.45 Å, Dissecting Therapeutic Resistance to ERK Inhibition Rat Wild Type SCH772984 in complex…
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

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