6MCQ: L. pneumophila effector kinase LegK7

L. pneumophila effector kinase LegK7 in complex with human MOB1A. Determined by X-ray diffraction at 2.57 Å resolution. Released 4 Sept 2019.

Method: X-ray diffraction
Resolution: 2.57 Å
Organisms: Legionella pneumophila subsp. pneumophila, Homo sapiens
Chains: 4
Atoms: 11,493
Mol. weight: 168.35 kDa
Ligands: ZN
Released: 4 Sept 2019

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

Secondary structure: helices and β-sheets

6MCQ contains 94 α-helices and 40 β-strands across 4 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: 37 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	14-22	9
α-helix	28-42	15
α-helix	46-47	2
α-helix	49-55	7
α-helix	63-68	6
β-strand	76	1	1
α-helix	78-91	14
α-helix	101-103	3
α-helix	106-119	14
α-helix	122-124	3
α-helix	126-142	17
α-helix	144-159	16
α-helix	161-168	8
β-strand	188-189	2	2
α-helix	190	1
β-strand	197	1	1
β-strand	206-210	5	1
α-helix	217-222	6
α-helix	226-230	5
β-strand	231	1	3
α-helix	232-233	2
β-strand	234-243	10	1
β-strand	249-258	10	1
α-helix	259-260	2
β-strand	264	1	4
α-helix	265-272	8
α-helix	277-279	3
α-helix	280-300	21
β-strand	304	1	5
α-helix	310-312	3
β-strand	314-316	3	4
β-strand	319-321	3	4
β-strand	322	1	3
β-strand	329	1	5
β-strand	335	1	6
α-helix	336-338	3
α-helix	343-345	3
α-helix	348-351	4
β-strand	354-356	3	7
β-strand	362-365	4	7
α-helix	367-370	4
β-strand	373	1	6
α-helix	376-394	19
α-helix	412-414	3
α-helix	420-432	13
α-helix	437-439	3
α-helix	441-442	2
α-helix	443-450	8
α-helix	457-467	11
α-helix	470-473	4
α-helix	476-487	12
α-helix	493-498	6
α-helix	500-505	6
α-helix	514-527	14

Chain B: 9 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	41-44	4
α-helix	53-75	23
β-strand	88	1	8
β-strand	94	1	8
β-strand	97	1	9
α-helix	106	1
β-strand	107	1	9
α-helix	111-126	16
α-helix	139-141	3
α-helix	144-172	29
α-helix	176-193	18
α-helix	202-204	3
α-helix	205-211	7

Chain C: 38 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	14-22	9
α-helix	28-42	15
α-helix	49-52	4
α-helix	63-68	6
α-helix	78-90	13
α-helix	101-103	3
α-helix	106-119	14
α-helix	122-124	3
α-helix	126-142	17
α-helix	144-159	16
α-helix	161-168	8
α-helix	172-174	3
α-helix	176-177	2
α-helix	181-183	3
β-strand	194-197	4	2
β-strand	206-210	5	2
α-helix	213-222	10
α-helix	226-230	5
β-strand	231	1	10
α-helix	232-233	2
β-strand	234-243	10	2
β-strand	249-258	10	2
β-strand	264	1	11
α-helix	265-271	7
α-helix	272-274	3
α-helix	277-279	3
α-helix	280-300	21
β-strand	304	1	12
α-helix	310-312	3
β-strand	314-316	3	11
β-strand	319-321	3	11
β-strand	322	1	10
β-strand	329	1	12
β-strand	335	1	13
α-helix	336-338	3
α-helix	348-351	4
β-strand	354-356	3	14
β-strand	362-365	4	14
α-helix	367-370	4
β-strand	373	1	13
α-helix	376-394	19
α-helix	412-414	3
α-helix	420-432	13
α-helix	437-439	3
α-helix	441-442	2
α-helix	443-449	7
α-helix	450-452	3
α-helix	457-467	11
α-helix	471-473	3
α-helix	476-486	11
α-helix	493-497	5
α-helix	500-505	6
α-helix	514-527	14

Chain D: 10 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	41-44	4
α-helix	53-75	23
β-strand	88	1	15
β-strand	94	1	15
β-strand	97	1	16
α-helix	105-106	2
β-strand	107	1	16
α-helix	111-126	16
α-helix	139-141	3
α-helix	144-165	22
α-helix	167-172	6
α-helix	176-193	18
α-helix	202-204	3
α-helix	205-210	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
LegK7	A, C	protein	523	Legionella pneumophila subsp. pneumophila	Q5ZU83 (AlphaFold model)
MOB kinase activator 1A	B, D	protein	187	Homo sapiens	Q9H8S9 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>6MCQ_1 LegK7 (chains A, C)
SNAKNTMPLVIAYNNAPEDDKIQKLFYLQKINYLLNKTQLNDDLFDWINDAEEGGWLNEL
AKFSINPNASFFLKGMQFAKAITEEIKNKPEINSSEVNIYHLMQERDQLLKEVEFEKCAT
RYAEINFLLNELALNDKKTKEIVERQTEILRLVAPKIKAIKGESIDNLPVIPSYKTKELG
NHVNNFNFKFTMSGWEAPFVFRVEDRHELGKEQELHSYGVSKYFIEDYSVFMMRFKAEDG
STVYKPVILSQFANQNNLEEIAKQLKDGSPKNIAPRIGYYFVQLTDFCLKLIETHNYHPD
IKLNNFLVHNNRVLVSDRKTFTTNDNPLASEILTSPLFAPDEFLKCLLFNKEGDPVGYNR
NALWKRMNMPQFMAYQLGMALKQFLILTQLDELPDDFRNPDHSAVSHFKTPSRQIINLSL
LVQELTRLDPDKRMTIKQFQTLLNFKNLPPDAFYQKVEEVFPSSQLGIAEDIEALNKVLN
SDLKGEALLKQANPVFTKLSKYDPKETRLTRLAEKLAIRCFNN

Sequence of entity 2 (B, D), FASTA

>6MCQ_2 MOB kinase activator 1A (chains B, D)
SNAEATLGSGNLRQAVMLPEGEDLNEWIAVNTVDFFNQINMLYGTITEFCTEASCPVMSA
GPRYEYHWADGTNIKKPIKCSAPKYIDYLMTWVQDQLDDETLFPSKIGVPFPKNFMSVAK
TILKRLFRVYAHIYHQHFDSVMQLQEEAHLNTSFKHFIFFVQEFNLIDRRELAPLQELIE
KLGSKDR

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	2

Water and common crystallization additives (PEG, P6G, PG4) are not listed.

Primary citation

TheLegionellakinase LegK7 exploits the Hippo pathway scaffold protein MOB1A for allostery and substrate phosphorylation. Lee, P.C., Beyrakhova, K., Xu, C. et al. Proc Natl Acad Sci U S A (2020) 117:14433-14443. DOI 10.1073/pnas.2000497117 · PubMed

Other PDB entries of the same protein (UniProt Q5ZU83 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6MCP 2.5 Å, L. pneumophila effector kinase LegK7 (AMP-PNP bound) in complex with human MOB1A
7BYK 2.65 Å, Crystal structure of the Legionella pneumophila LegK7 effector kinase

Browse structure collections

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