2WTK: Heterotrimeric LKB1-STRADalpha-MO25alpha complex

Structure of the heterotrimeric LKB1-STRADalpha-MO25alpha complex. Determined by X-ray diffraction at 2.65 Å resolution. Released 15 Dec 2009.

Method: X-ray diffraction
Resolution: 2.65 Å
Organism: HOMO SAPIENS
Chains: 6
Atoms: 14,850
Mol. weight: 234.06 kDa
Ligands: ANP
Released: 15 Dec 2009

Explore 2WTK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2WTK contains 115 α-helices and 63 β-strands across 6 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: 23 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	12-26	15
α-helix	34-54	21
α-helix	64-77	14
α-helix	79-85	7
α-helix	87-89	3
α-helix	92-107	16
β-strand	110	1	1
β-strand	113	1	1
α-helix	115-121	7
α-helix	125-132	8
α-helix	133-135	3
α-helix	140-150	11
α-helix	154-161	8
α-helix	164-168	5
α-helix	169-172	4
α-helix	178-193	16
α-helix	196-218	23
α-helix	223-238	16
α-helix	240-242	3
α-helix	243-249	7
α-helix	253-262	10
α-helix	268-283	16
α-helix	289-297	9
α-helix	299-306	8
α-helix	319-331	13

Chain B: 17 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	66-68	3
β-strand	69-78	10	2
β-strand	83-90	8	2
β-strand	96-103	8	2
α-helix	109-124	16
β-strand	130	1	3
β-strand	133-138	6	2
β-strand	142-148	7	2
β-strand	153-154	2	3
α-helix	155-161	7
α-helix	169-188	20
β-strand	191-192	2	4
α-helix	198-200	3
β-strand	201-203	3	3
β-strand	209-211	3	3
α-helix	214-216	3
β-strand	218-219	2	4
β-strand	221-222	2	5
β-strand	225-226	2	5
β-strand	230	1	6
α-helix	238-243	6
α-helix	246-249	4
β-strand	256	1	6
α-helix	259-274	16
α-helix	284-289	6
α-helix	350-359	10
α-helix	364-366	3
α-helix	370-374	5
α-helix	377-379	3
α-helix	386-388	3
α-helix	390-392	3
α-helix	406-409	4

Chain C: 18 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	49	1	7
β-strand	54-57	4	8
β-strand	62-67	6	8
β-strand	68	1	7
β-strand	74-80	7	8
α-helix	82-87	6
α-helix	91-102	12
β-strand	110	1	9
α-helix	111-112	2
β-strand	113-118	6	8
β-strand	125-130	6	8
α-helix	131	1
β-strand	134-135	2	9
α-helix	136-142	7
α-helix	150-169	20
β-strand	172-173	2	10
α-helix	179-181	3
β-strand	182-184	3	9
β-strand	190-192	3	9
β-strand	199-200	2	10
α-helix	201-202	2
β-strand	209-210	2	11
α-helix	217-219	3
α-helix	222-225	4
β-strand	231-232	2	11
α-helix	234-250	17
α-helix	260-269	10
α-helix	280-289	10
α-helix	298-299	2
α-helix	300-305	6
α-helix	307-310	4
α-helix	312-314	3
α-helix	339-341	3

Chain D: 24 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	12-27	16
α-helix	33-55	23
α-helix	64-77	14
α-helix	79-85	7
α-helix	87-89	3
α-helix	92-106	15
β-strand	110	1	12
β-strand	113	1	12
α-helix	115-121	7
α-helix	125-132	8
α-helix	133-135	3
α-helix	140-150	11
α-helix	154-161	8
α-helix	164-168	5
α-helix	169-172	4
α-helix	178-193	16
α-helix	196-205	10
α-helix	207-218	12
α-helix	223-238	16
α-helix	240-242	3
α-helix	243-249	7
α-helix	253-262	10
α-helix	268-283	16
α-helix	289-297	9
α-helix	299-308	10
α-helix	318-331	14

Chain E: 19 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	70-78	9	13
α-helix	79-81	3
β-strand	83-90	8	13
β-strand	95-103	9	13
α-helix	104-106	3
α-helix	109-124	16
β-strand	130	1	14
α-helix	131-132	2
β-strand	133-138	6	13
β-strand	142-148	7	13
β-strand	154	1	14
α-helix	155-161	7
α-helix	169-188	20
β-strand	191-192	2	15
α-helix	198-200	3
β-strand	201-203	3	14
β-strand	209-211	3	14
α-helix	214-216	3
β-strand	218-219	2	15
β-strand	221-222	2	16
β-strand	225-226	2	16
β-strand	230	1	17
α-helix	233-234	2
α-helix	241-243	3
α-helix	246-249	4
β-strand	256	1	17
α-helix	259-274	16
α-helix	284-291	8
α-helix	350-359	10
α-helix	364-366	3
α-helix	370-373	4
α-helix	377-381	5
α-helix	390-393	4
α-helix	406-408	3

Chain F: 14 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	46	1	18
β-strand	49-57	9	18
β-strand	62-68	7	18
β-strand	74-79	6	18
α-helix	82-86	5
α-helix	91-103	13
β-strand	110	1	19
α-helix	111-112	2
β-strand	113-117	5	18
β-strand	126-130	5	18
β-strand	134-135	2	19
α-helix	136-140	5
α-helix	150-169	20
β-strand	172-173	2	20
α-helix	179-181	3
β-strand	182-184	3	19
β-strand	190-192	3	19
β-strand	199-200	2	20
α-helix	201-202	2
β-strand	209-210	2	21
α-helix	217-219	3
β-strand	231-232	2	21
α-helix	233-250	18
α-helix	263-267	5
α-helix	283-289	7
α-helix	298-299	2
α-helix	300-305	6
α-helix	307-310	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Calcium-binding protein 39	A, D	protein	341	HOMO SAPIENS	Q9Y376 (AlphaFold model)
STE20-related kinase adapter protein alpha	B, E	protein	373	HOMO SAPIENS	Q7RTN6 (AlphaFold model)
Serine/threonine-protein kinase 11	C, F	protein	305	HOMO SAPIENS	Q15831 (AlphaFold model)

Sequence of entity 1 (A, D), FASTA

>2WTK_1 CALCIUM-BINDING PROTEIN 39 (chains A, D)
MPFPFGKSHKSPADIVKNLKESMAVLEKQDISDKKAEKATEEVSKNLVAMKEILYGTNEK
EPQTEAVAQLAQELYNSGLLSTLVADLQLIDFEGKKDVAQIFNNILRRQIGTRTPTVEYI
CTQQNILFMLLKGYESPEIALNCGIMLRECIRHEPLAKIILWSEQFYDFFRYVEMSTFDI
ASDAFATFKDLLTRHKLLSAEFLEQHYDRFFSEYEKLLHSENYVTKRQSLKLLGELLLDR
HNFTIMTKYISKPENLKLMMNLLRDKSRNIQFEAFHVFKVFVANPNKTQPILDILLKNQA
KLIEFLSKFQNDRTEDEQFNDEKTYLVKQIRDLKRPAQQEA

Sequence of entity 2 (B, E), FASTA

>2WTK_2 STE20-RELATED KINASE ADAPTER PROTEIN ALPHA (chains B, E)
MSSFLPEGGCYELLTVIGKGFEDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGE
LHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFMDGMNELAIAYILQG
VLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISHGQRQRVVHDFPKYSV
KVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPC
LLDTSTIPAEELTMSPSRSVANSGLSDSLTTSTPRPSNGDSPSHPYHRTFSPHFHHFVEQ
CLQRNPDARPSASTLLNHSFFKQIKRRASEALPELLRPVTPITNFEGSQSQDHSGIFGLV
TNLEELEVDDWEF

Sequence of entity 3 (C, F), FASTA

>2WTK_3 SERINE/THREONINE-PROTEIN KINASE 11 (chains C, F)
AKLIGKYLMGDLLGEGSYGKVKEVLDSETLCRRAVKILKKKKLRRIPNGEANVKKEIQLL
RRLRHKNVIQLVDVLYNEEKQKMYMVMEYCVCGMQEMLDSVPEKRFPVCQAHGYFCQLID
GLEYLHSQGIVHKDIKPGNLLLTTGGTLKISALGVAEALHPFAADDTCRTSQGSPAFQPP
EIANGLDTFSGFKVDIWSAGVTLYNITTGLYPFEGDNIYKLFENIGKGSYAIPGDCGPPL
SDLLKGMLEYEPAKRFSIRQIRQHSWFRKKHPPAEAPVPIPPSPDTKDRWRSMTVVPYLE
DLHGA

Ligands and cofactors

ID	Name	Formula	Copies
ANP	Phosphoaminophosphonic acid-adenylate ester	C10 H17 N6 O12 P3	4

Water and common crystallization additives (SO4) are not listed.

Primary citation

Structure of the Lkb1-Strad-Mo25 Complex Reveals an Allosteric Mechanism of Kinase Activation. Zeqiraj, E., Filippi, B.M., Deak, M. et al. Science (2009) 326:1707. DOI 10.1126/SCIENCE.1178377 · PubMed

Other PDB entries of the same protein (UniProt Q9Y376 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1UPK 1.85 Å, Crystal structure of MO25 in complex with a C-terminal peptide of STRAD
3GNI 2.35 Å, Structure of STRAD and MO25
1UPL 2.6 Å, Crystal structure of MO25 alpha
8VSU 2.86 Å, Cryo-EM structure of LKB1-STRADalpha-MO25alpha heterocomplex
4FZA 3.15 Å, Crystal structure of MST4-MO25 complex
4O27 3.19 Å, Crystal structure of MST3-MO25 complex with WIF motif
4FZD 3.25 Å, Crystal structure of MST4-MO25 complex with WSF motif
4NZW 3.58 Å, Crystal Structure of STK25-MO25 Complex
4FZF 3.64 Å, Crystal structure of MST4-MO25 complex with DKI

Browse structure collections

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