6MCP: L. pneumophila effector kinase LegK7

L. pneumophila effector kinase LegK7 (AMP-PNP bound) in complex with human MOB1A. Determined by X-ray diffraction at 2.5 Å resolution. Released 4 Sept 2019.

Method
X-ray diffraction
Resolution
2.5 Å
Organisms
Legionella pneumophila subsp. pneumophila, Homo sapiens
Chains
4
Atoms
11,356
Mol. weight
169.02 kDa
Ligands
ZN, MN, ANP
Released
4 Sept 2019

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

Secondary structure: helices and β-sheets

6MCP contains 92 α-helices and 42 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: 36 helices, 17 β-strands

ElementResiduesLengthSheet
α-helix14-229
α-helix28-4215
α-helix49-557
α-helix63-697
β-strand7611
α-helix78-9013
α-helix106-11914
α-helix122-1243
α-helix126-14217
α-helix144-15916
α-helix161-1688
β-strand188-18922
α-helix1901
β-strand19711
β-strand206-21051
α-helix217-2226
α-helix226-2305
β-strand23113
α-helix232-2332
β-strand234-243101
β-strand249-258101
α-helix259-2602
β-strand26414
α-helix265-2717
α-helix272-2743
α-helix277-2793
α-helix280-30021
β-strand30415
α-helix310-3123
β-strand314-31634
β-strand319-32134
β-strand32213
β-strand32915
β-strand33516
α-helix336-3383
α-helix348-3514
β-strand354-35637
α-helix358-3603
β-strand362-36547
α-helix367-3704
β-strand37316
α-helix376-39419
α-helix411-4144
α-helix420-43213
α-helix437-4393
α-helix441-4422
α-helix443-4508
α-helix457-46711
α-helix470-4734
α-helix476-48611
α-helix493-50715
α-helix512-5132
α-helix514-52714
Chain B: 11 helices, 4 β-strands
ElementResiduesLengthSheet
α-helix41-444
α-helix47-482
α-helix53-7523
β-strand8818
β-strand9418
β-strand96-9729
α-helix105-1062
β-strand107-10829
α-helix111-12717
α-helix139-1413
α-helix144-17229
α-helix176-19318
α-helix198-2014
α-helix202-2043
α-helix205-2128
Chain C: 34 helices, 17 β-strands
ElementResiduesLengthSheet
α-helix14-229
α-helix28-4215
α-helix49-557
α-helix63-697
β-strand7612
α-helix78-9013
α-helix106-11914
α-helix122-1243
α-helix126-14217
α-helix144-15916
α-helix161-1699
α-helix1761
β-strand17712
β-strand194-19742
β-strand206-21052
α-helix213-22210
α-helix226-2305
β-strand231110
α-helix232-2332
β-strand234-243102
β-strand249-258102
α-helix259-2602
β-strand264111
α-helix265-2717
α-helix272-2743
α-helix277-2793
α-helix280-30021
β-strand304112
α-helix310-3123
β-strand314-316311
β-strand319-321311
β-strand322110
β-strand329112
β-strand335113
α-helix336-3383
α-helix348-3514
β-strand354-356314
β-strand362-365414
α-helix367-3704
β-strand373113
α-helix376-39419
α-helix411-4144
α-helix420-43213
α-helix437-4393
α-helix441-4422
α-helix443-4508
α-helix457-46711
α-helix470-4734
α-helix476-48611
α-helix493-50715
α-helix514-52714
Chain D: 11 helices, 4 β-strands
ElementResiduesLengthSheet
α-helix41-444
α-helix47-482
α-helix53-7523
β-strand88115
β-strand94115
β-strand97116
α-helix105-1062
β-strand107116
α-helix111-12717
α-helix138-1414
α-helix144-17229
α-helix176-19318
α-helix198-2014
α-helix202-2043
α-helix205-2106

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
LegK7A, Cprotein523Legionella pneumophila subsp. pneumophilaQ5ZU83 (AlphaFold model)
MOB kinase activator 1AB, Dprotein187Homo sapiensQ9H8S9 (AlphaFold model)
Sequence of entity 1 (A, C), FASTA
>6MCP_1 LegK7 (chains A, C)
SNAKNTMPLVIAYNNAPEDDKIQKLFYLQKINYLLNKTQLNDDLFDWINDAEEGGWLNEL
AKFSINPNASFFLKGMQFAKAITEEIKNKPEINSSEVNIYHLMQERDQLLKEVEFEKCAT
RYAEINFLLNELALNDKKTKEIVERQTEILRLVAPKIKAIKGESIDNLPVIPSYKTKELG
NHVNNFNFKFTMSGWEAPFVFRVEDRHELGKEQELHSYGVSKYFIEDYSVFMMRFKAEDG
STVYKPVILSQFANQNNLEEIAKQLKDGSPKNIAPRIGYYFVQLTDFCLKLIETHNYHPD
IKLNNFLVHNNRVLVSDRKTFTTNDNPLASEILTSPLFAPDEFLKCLLFNKEGDPVGYNR
NALWKRMNMPQFMAYQLGMALKQFLILTQLDELPDDFRNPDHSAVSHFKTPSRQIINLSL
LVQELTRLDPDKRMTIKQFQTLLNFKNLPPDAFYQKVEEVFPSSQLGIAEDIEALNKVLN
SDLKGEALLKQANPVFTKLSKYDPKETRLTRLAEKLAIRCFNN
Sequence of entity 2 (B, D), FASTA
>6MCP_2 MOB kinase activator 1A (chains B, D)
SNAEATLGSGNLRQAVMLPEGEDLNEWIAVNTVDFFNQINMLYGTITEFCTEASCPVMSA
GPRYEYHWADGTNIKKPIKCSAPKYIDYLMTWVQDQLDDETLFPSKIGVPFPKNFMSVAK
TILKRLFRVYAHIYHQHFDSVMQLQEEAHLNTSFKHFIFFVQEFNLIDRRELAPLQELIE
KLGSKDR

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2
MNManganese (II) ionMn1
ANPPhosphoaminophosphonic acid-adenylate esterC10 H17 N6 O12 P31

Water and common crystallization additives (PG4, PEG, P6G) 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:

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