5BYZ: ERK5

ERK5 in complex with small molecule. Determined by X-ray diffraction at 1.65 Å resolution. Released 4 May 2016.

Method: X-ray diffraction
Resolution: 1.65 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,367
Mol. weight: 40.84 kDa
Ligands: 4WE
Released: 4 May 2016

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

Secondary structure: helices and β-sheets

5BYZ contains 27 α-helices and 11 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: 27 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	55-64	10	1
β-strand	67-74	8	1
β-strand	80-86	7	1
α-helix	93-108	16
β-strand	114	1	2
β-strand	117-120	4	1
α-helix	121-123	3
α-helix	127-129	3
β-strand	133-137	5	1
β-strand	142-143	2	2
α-helix	144-148	5
α-helix	156-175	20
β-strand	179	1	3
α-helix	185-187	3
β-strand	188-190	3	2
β-strand	196-198	3	2
β-strand	205	1	3
α-helix	214-216	3
α-helix	219-221	3
α-helix	225-227	3
α-helix	230-234	5
α-helix	242-257	16
α-helix	267-278	12
α-helix	281-282	2
α-helix	283-287	5
α-helix	292-300	9
α-helix	302-303	2
α-helix	305-308	4
α-helix	309-312	4
α-helix	318-327	10
α-helix	332-334	3
α-helix	336-337	2
α-helix	338-342	5
α-helix	345-347	3
α-helix	353-355	3
α-helix	362-364	3
α-helix	366-369	4
α-helix	374-393	20

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mitogen-activated protein kinase 7	A	protein	348	Homo sapiens	Q13164 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5BYZ_1 Mitogen-activated protein kinase 7 (chains A)
TFDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILK
HFKHDNIIAIKDILRPTVPYGEFKSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLL
RGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPAEHQYFMTEYVATRWY
RAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQ
AVGAERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFL
AKYHDPDDEPDCAPPFDFAFDREALTRERIKEAIVAEIEDFHARREGI

Ligands and cofactors

ID	Name	Formula	Copies
4WE	4-({5-fluoro-4-[2-methyl-1-(propan-2-yl)-1H-imidazol-5-yl]pyrimidin-2-yl}amino)…	C25 H32 F N7 O	1

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

Primary citation

Discovery of a novel allosteric inhibitor-binding site in ERK5: comparison with the canonical kinase hinge ATP-binding site. Chen, H., Tucker, J., Wang, X. et al. Acta Crystallogr D Struct Biol (2016) 72:682-693. DOI 10.1107/S2059798316004502 · PubMed

Other PDB entries of the same protein (UniProt Q13164 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4ZSG 1.79 Å, Mitogen activated protein kinase 7 in complex with inhibitor
2Q8Y 2.0 Å, Structural insight into the enzymatic mechanism of the phophothreonine lyase
4ZSL 2.25 Å, Mitogen activated protein kinase 7 in complex with inhibitor
6HKN 2.33 Å, Crystal structure of Compound 35 with ERK5
9LTA 2.33 Å, Crystal Structure of Compound SKLB-D18 with MAPK7 (ERK5)
5O7I 2.38 Å, ERK5 in complex with a pyrrole inhibitor
6HKM 2.47 Å, Crystal structure of Compound 1 with ERK5
4ZSJ 2.48 Å, Mitogen activated protein kinase 7 in complex with inhibitor
7PUS 2.59 Å, ERK5 in complex with Pyrrole Carboxamide scaffold
4IC7 2.6 Å, Crystal structure of the ERK5 kinase domain in complex with an MKK5 binding fragment
5BYY 2.79 Å, ERK5 in complex with small molecule
4B99 2.8 Å, Crystal Structure of MAPK7 (ERK5) with inhibitor

Browse structure collections

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