4IC8: Apo ERK5 kinase domain

Crystal structure of the apo ERK5 kinase domain. Determined by X-ray diffraction at 2.8 Å resolution. Released 13 Feb 2013.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 2
Atoms: 4,807
Mol. weight: 99.61 kDa
Released: 13 Feb 2013

Explore 4IC8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4IC8 contains 28 α-helices and 20 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: 14 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	33-37	5	1
β-strand	47-52	6	1
β-strand	58-63	6	1
α-helix	73-86	14
β-strand	89	1	2
β-strand	92	1	2
β-strand	97-99	3	1
β-strand	112-116	5	1
β-strand	120-121	2	2
α-helix	122-125	4
α-helix	134-153	20
α-helix	163-165	3
β-strand	166-168	3	2
β-strand	174-176	3	2
α-helix	221-235	15
α-helix	245-256	12
α-helix	271-278	8
α-helix	287-290	4
α-helix	296-305	10
α-helix	316-320	5
α-helix	323-325	3
α-helix	331-333	3
α-helix	340-342	3
α-helix	354-358	5

Chain B: 14 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	33-34	2	3
β-strand	38-41	4	3
β-strand	46-52	7	3
β-strand	57-63	7	3
α-helix	71-86	16
β-strand	92	1	4
β-strand	97-99	3	3
α-helix	100-101	2
β-strand	112-116	5	3
β-strand	120-121	2	4
α-helix	134-153	20
α-helix	163-165	3
β-strand	166-169	4	4
β-strand	173-176	4	4
α-helix	221-235	15
α-helix	245-256	12
α-helix	271-278	8
α-helix	287-290	4
α-helix	296-305	10
α-helix	316-320	5
α-helix	325-327	3
α-helix	331-333	3
α-helix	340-341	2
α-helix	355-361	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mitogen-activated protein kinase 7	A, B	protein	442	Homo sapiens	Q13164 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4IC8_1 Mitogen-activated protein kinase 7 (chains A, B)
GSMAEPLKEEDGEDGSAEPPGPVKAEPAHTAASVAAKNLALLKARSFDVTFDVGDEYEII
ETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIK
DILRPTVPYGEFKSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQV
IHRDLKPSNLLVNENCELKIGDFGMARGLCTSPAEHQYFMTEYVATRWYRAPELMLSLHE
YTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQAVGAERVRAYI
QSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFLAKYHDPDDEPD
CAPPFDFAFDREALTRERIKEAIVAEIEDFHARREGIRQQIRFQPSLQPVASEPGCPDVE
MPSPWAPSGDCAMSGRHHHHHH

Primary citation

Structural mechanism for the specific assembly and activation of the extracellular signal regulated kinase 5 (ERK5) module. Glatz, G., Gogl, G., Alexa, A. et al. J Biol Chem (2013) 288:8596-8609. DOI 10.1074/jbc.M113.452235 · PubMed

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

5BYZ 1.65 Å, ERK5 in complex with small molecule
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

Browse structure collections

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