2Y9Q: Human ERK2

Crystal structure of human ERK2 complexed with a MAPK docking peptide. Determined by X-ray diffraction at 1.55 Å resolution. Released 29 Feb 2012.

Method: X-ray diffraction
Resolution: 1.55 Å
Organism: HOMO SAPIENS
Chains: 2
Atoms: 3,632
Mol. weight: 44.14 kDa
Ligands: ANP
Released: 29 Feb 2012

Explore 2Y9Q in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2Y9Q contains 25 α-helices and 15 β-strands across 2 chains. 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: 22 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	13-14	2	1
β-strand	17-18	2	1
β-strand	25-33	9	2
β-strand	38-44	7	2
β-strand	49-56	8	2
α-helix	62-77	16
β-strand	83	1	3
β-strand	88-90	3	2
β-strand	101-106	6	2
β-strand	110-111	2	3
α-helix	112-118	7
α-helix	120-122	3
α-helix	123-142	20
β-strand	145-146	2	4
α-helix	152-154	3
β-strand	155-157	3	3
β-strand	163-165	3	3
β-strand	172-173	2	4
β-strand	179	1	5
α-helix	196-200	5
β-strand	203	1	5
α-helix	208-223	16
α-helix	233-244	12
α-helix	246-248	3
α-helix	249-252	4
α-helix	258-266	9
α-helix	268-269	2
α-helix	271-274	4
α-helix	275-278	4
α-helix	284-293	10
α-helix	298-300	3
α-helix	302-303	2
α-helix	304-308	5
α-helix	311-313	3
α-helix	319-321	3
α-helix	340-351	12
α-helix	352-354	3

Chain B: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	436-438	3
α-helix	439-441	3
α-helix	443-449	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mitogen-activated protein kinase 1	A	protein	362	HOMO SAPIENS	P28482 (AlphaFold model)
Map kinase-interacting serine/threonine-protein kinase 1	B	protein	18	HOMO SAPIENS	Q9BUB5 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2Y9Q_1 MITOGEN-ACTIVATED PROTEIN KINASE 1 (chains A)
GSMAAAAAAGAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNVNKVRVAIKKISP
FEHQTYCQRTLREIKILLRFRHENIIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKT
QHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADPDH
DHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLN
HILGILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNP
HKRIEVEQALAHPYLEQYYDPSDEPIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGY
RS

Sequence of entity 2 (B), FASTA

>2Y9Q_2 MAP KINASE-INTERACTING SERINE/THREONINE-PROTEIN KINASE 1 (chains B)
MKLSPPSKSRLARRRALA

Ligands and cofactors

ID	Name	Formula	Copies
ANP	Phosphoaminophosphonic acid-adenylate ester	C10 H17 N6 O12 P3	1

Primary citation

Specificity of Linear Motifs that Bind to a Common Mitogen-Activated Protein Kinase Docking Groove. Garai, A., Zeke, A., Gogl, G. et al. Sci Signal (2012) 5:74. DOI 10.1126/SCISIGNAL.2003004 · PubMed

Other PDB entries of the same protein (UniProt P28482 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8AOJ 1.12 Å, Specific covalent inhibitor of ERK2
4ZZN 1.33 Å, Human ERK2 in complex with an inhibitor
6SLG 1.33 Å, Human ERK2 with ERK1/2 inhibitor, AZD0364.
5WP1 1.4 Å, Complex of ERK2 with 5,7-dihydroxychromone
4QTA 1.45 Å, Structure of human ERK2 in complex with SCH772984 revealing a novel inhibitor-induced…
4QTE 1.5 Å, Structure of ERK2 in complex with VTX-11e, 4-{2-[(2-CHLORO-4-FLUOROPHENYL)AMINO]-5-METHYL…
6QA3 1.57 Å, ERK2 mini-fragment binding
6QAL 1.57 Å, ERK2 mini-fragment binding
6GJD 1.58 Å, Erk2 signalling protein
6QA1 1.58 Å, ERK2 mini-fragment binding
6QAH 1.58 Å, ERK2 mini-fragment binding
6QAQ 1.58 Å, ERK2 mini-fragment binding

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