5Y90: MAP2K7 mutant -C218S

MAP2K7 mutant -C218S. Determined by X-ray diffraction at 1.3 Å resolution. Released 11 Oct 2017.

Method: X-ray diffraction
Resolution: 1.3 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,925
Mol. weight: 37.22 kDa
Released: 11 Oct 2017

Explore 5Y90 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5Y90 contains 19 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: 19 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	120-124	5	1
β-strand	127-131	5	1
α-helix	133-135	3
β-strand	137-142	6	1
β-strand	149-154	6	1
β-strand	161-168	8	1
α-helix	173-187	15
β-strand	195	1	2
α-helix	196-197	2
β-strand	198-203	6	1
β-strand	207-212	6	1
β-strand	217-218	2	2
α-helix	219-226	8
α-helix	229-231	3
α-helix	232-253	22
α-helix	262-264	3
β-strand	265-267	3	2
β-strand	273-275	3	2
α-helix	297-299	3
α-helix	302-305	4
α-helix	318-333	16
α-helix	344-353	10
α-helix	355-357	3
α-helix	367-376	10
α-helix	381-383	3
α-helix	385-386	2
α-helix	387-390	4
α-helix	394-401	8
α-helix	406-417	12
α-helix	426-433	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Dual specificity mitogen-activated protein kinase kinase 7	A	protein	323	Homo sapiens	O14733 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5Y90_1 Dual specificity mitogen-activated protein kinase kinase 7 (chains A)
TGYLTIGGQRYQAEINDLENLGEMGSGTCGQVWKMRFRKTGHVIAVKQMRRSGNKEENKR
ILMDLDVVLKSHDCPYIVQCFGTFITNTDVFIAMELMGTSAEKLKKRMQGPIPERILGKM
TVAIVKALYYLKEKHGVIHRDVKPSNILLDERGQIKLCDFGISGRLVDSKAKTRSAGCAA
YMAPERIDPPDPTKPDYDIRADVWSLGISLVELATGQFPYKNCKTDFEVLTKVLQEEPPL
LPGHMGFSGDFQSFVKDCLTKDHRKRPKYNKLLEHSFIKRYETLEVDVASWFKDVMAKTE
SPRTSGVLSQPHLPFFRHHHHHH

Primary citation

High-resolution structure discloses the potential for allosteric regulation of mitogen-activated protein kinase kinase 7. Kinoshita, T., Hashimoto, T., Sogabe, Y. et al. Biochem Biophys Res Commun (2017) 493:313-317. DOI 10.1016/j.bbrc.2017.09.025 · PubMed

Other PDB entries of the same protein (UniProt O14733 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6YZ4 1.7 Å, Crystal structure of MKK7 (MAP2K7) with ibrutinib bound at allosteric site
6YFZ 1.9 Å, Crystal structure of MKK7 (MAP2K7), apo form
7OVI 1.95 Å, Protein kinase MKK7 in complex with phenethyltriazole-substituted pyrazolopyrimidine
6YG0 2.0 Å, Crystal structure of S287D,T291D MKK7 (MAP2K7), apo form
6YG2 2.0 Å, Crystal structure of MKK7 (MAP2K7) in complex with ibrutnib, with covalent and…
6YG3 2.05 Å, Crystal structure of MKK7 (MAP2K7) covalently bound with CPT1-70-1
7OVK 2.05 Å, Protein kinase MKK7 in complex with 5-bromo-2-hydroxyphenyl-substituted pyrazolopyrimidine
7CBX 2.06 Å, Crystal structure of MAP2K7 complexed with a covalent inhibitor 12
5B2L 2.1 Å, A crucial role of Cys218 in the stabilization of an unprecedented auto-inhibition form…
6IB2 2.1 Å, The structure of MKK7 in complex with the covalent 4-amino-pyrazolopyrimidine 4a
6QG7 2.1 Å, Structure of the mitogen activated kinase kinase 7 in complex with pyrazolopyrimidine 1k
6YG6 2.15 Å, Crystal structure of MKK7 (MAP2K7) covalently bound with type-II inhibitor TL10-105

Browse structure collections

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