6QFR: PDB entry 6QFR

Structure of the mitogen activated kinase kinase 7 dfg-out conformation. Determined by X-ray diffraction at 2.3 Å resolution. Released 22 May 2019.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,118
Mol. weight: 36.15 kDa
Released: 22 May 2019

Explore 6QFR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6QFR contains 16 α-helices and 12 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: 16 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	119	1	1
β-strand	121-124	4	2
β-strand	127-130	4	2
α-helix	133-135	3
β-strand	136-141	6	1
β-strand	150-155	6	1
β-strand	161-168	8	1
α-helix	173-188	16
β-strand	195	1	3
α-helix	196-197	2
β-strand	198-203	6	1
β-strand	207-212	6	1
β-strand	217-218	2	3
α-helix	219-226	8
α-helix	229-231	3
α-helix	232-251	20
α-helix	262-264	3
β-strand	265-267	3	3
β-strand	273-275	3	3
α-helix	319-333	15
α-helix	344-353	10
α-helix	355-356	2
α-helix	358-360	3
α-helix	367-376	10
α-helix	381-383	3
α-helix	387-390	4
α-helix	394-401	8
α-helix	406-415	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Dual specificity mitogen-activated protein kinase kinase 7	A	protein	318	Homo sapiens	O14733 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6QFR_1 Dual specificity mitogen-activated protein kinase kinase 7 (chains A)
MGHHHHHHSAKQTGYLTIGGQRYQAEINDLENLGEMGSGTCGQVWKMRFRKTGHVIAVKQ
MRRSGNKEENKRILMDLDVVLKSHDCPYIVQCFGTFITNTDVFIAMELMGTCAEKLKKRM
QGPIPERILGKMTVAIVKALYYLKEKHGVIHRDVKPSNILLDERGQIKLCDFGISGRLVD
SKAKTRSAGCAAYMAPERIDPPDPTKPDYDIRADVWSLGISLVELATGQFPYKNCKTDFE
VLTKVLQEEPPLLPGHMGFSGDFQSFVKDCLTKDHRKRPKYNKLLEHSFIKRYETLEVDV
ASWFKDVMAKTESPRTSG

Primary citation

Characterization of Covalent Pyrazolopyrimidine-MKK7 Complexes and a Report on a Unique DFG-in/Leu-in Conformation of Mitogen-Activated Protein Kinase Kinase 7 (MKK7). Wolle, P., Engel, J., Smith, S. et al. J Med Chem (2019) 62:5541-5546. DOI 10.1021/acs.jmedchem.9b00472 · PubMed

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

5Y90 1.3 Å, MAP2K7 mutant -C218S
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

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