4ZZN: Human ERK2

Human ERK2 in complex with an inhibitor. Determined by X-ray diffraction at 1.33 Å resolution. Released 27 May 2015.

Method: X-ray diffraction
Resolution: 1.33 Å
Organism: HOMO SAPIENS
Chains: 1
Atoms: 3,153
Mol. weight: 41.25 kDa
Ligands: CQ8
Released: 27 May 2015

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

Secondary structure: helices and β-sheets

4ZZN 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	11-12	2	1
β-strand	15-16	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
α-helix	105-106	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	233-242	10
α-helix	245-246	2
α-helix	247-251	5
α-helix	256-263	8
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	338-349	12
α-helix	350-352	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mitogen-activated protein kinase 1	A	protein	350	HOMO SAPIENS	P28482 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4ZZN_1 MITOGEN-ACTIVATED PROTEIN KINASE 1 (chains A)
PEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNLNKVRVAIKKISPFEHQTYCQRTLR
EIKILLRFRHENIIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFL
YQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADPDHDHTGFLTEYVAT
RWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQE
DLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAH
PYLEQYYDPSDEPIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGYRS

Ligands and cofactors

ID	Name	Formula	Copies
CQ8	2-[[5-chloranyl-2-(oxan-4-ylamino)pyridin-4-yl]amino]-N-methyl-benzamide	C18 H21 Cl N4 O2	1

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

Primary citation

Structure-Guided Design of Highly Selective and Potent Covalent Inhibitors of Erk1/2. Ward, R.A., Colclough, N., Challinor, M. et al. J Med Chem (2015) 58:4790. DOI 10.1021/ACS.JMEDCHEM.5B00466 · 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
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…
2Y9Q 1.55 Å, Crystal structure of human ERK2 complexed with a MAPK docking peptide
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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