3IEC: Serine/threonine-protein kinase MARK2

Helicobacter pylori CagA Inhibits PAR1/MARK Family Kinases by Mimicking Host Substrates. Determined by X-ray diffraction at 2.2 Å resolution. Released 8 Dec 2009.

Method: X-ray diffraction
Resolution: 2.2 Å
Organisms: Homo sapiens, Helicobacter pylori
Chains: 8
Atoms: 11,312
Mol. weight: 201.37 kDa
Released: 8 Dec 2009

Explore 3IEC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3IEC contains 72 α-helices and 78 β-strands across 8 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: 18 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	50	1	1
β-strand	53-58	6	1
β-strand	66-72	7	1
β-strand	78-85	8	1
α-helix	91-106	16
β-strand	112	1	2
α-helix	113-114	2
β-strand	115-120	6	1
β-strand	124-129	6	1
β-strand	135-136	2	2
α-helix	137-144	8
α-helix	149-168	20
β-strand	171-172	2	3
α-helix	178-180	3
β-strand	181-183	3	2
β-strand	189-191	3	2
β-strand	198-199	2	3
β-strand	206	1	4
β-strand	211	1	5
α-helix	213-215	3
α-helix	218-221	4
β-strand	226	1	4
α-helix	228-245	18
β-strand	247	1	6
α-helix	255-264	10
α-helix	275-284	10
α-helix	289-291	3
α-helix	293-294	2
α-helix	295-299	5
α-helix	302-305	4
α-helix	318-321	4
α-helix	326-334	9
α-helix	339-347	9
α-helix	353-361	9

Chain B: 18 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	50	1	7
β-strand	53-60	8	7
β-strand	66-72	7	7
β-strand	78-85	8	7
α-helix	91-106	16
β-strand	112	1	8
α-helix	113-114	2
β-strand	115-120	6	7
β-strand	124-129	6	7
β-strand	135-136	2	8
α-helix	137-144	8
α-helix	149-168	20
β-strand	171-172	2	9
α-helix	178-180	3
β-strand	181-183	3	8
β-strand	189-191	3	8
β-strand	198-199	2	9
β-strand	201	1	10
β-strand	204	1	10
β-strand	206	1	11
β-strand	211	1	12
α-helix	213-215	3
α-helix	218-222	5
β-strand	226	1	11
α-helix	228-245	18
β-strand	247	1	13
α-helix	255-264	10
α-helix	275-284	10
α-helix	289-291	3
α-helix	293-294	2
α-helix	295-298	4
α-helix	302-305	4
α-helix	315-321	7
α-helix	326-334	9
α-helix	339-347	9
α-helix	353-362	10

Chain C: 18 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	50	1	14
β-strand	53-58	6	14
β-strand	66-72	7	14
β-strand	78-85	8	14
α-helix	91-106	16
β-strand	112	1	15
α-helix	113-114	2
β-strand	115-120	6	14
β-strand	124-129	6	14
β-strand	135-136	2	15
α-helix	137-144	8
α-helix	149-168	20
β-strand	171-172	2	16
α-helix	178-180	3
β-strand	181-183	3	15
β-strand	189-191	3	15
β-strand	198-199	2	16
β-strand	201	1	17
β-strand	204	1	17
β-strand	206	1	18
β-strand	211	1	19
α-helix	213-215	3
α-helix	218-222	5
β-strand	226	1	18
α-helix	229-245	17
β-strand	247	1	20
α-helix	255-264	10
α-helix	275-284	10
α-helix	289-291	3
α-helix	293-294	2
α-helix	295-298	4
α-helix	302-305	4
α-helix	318-321	4
α-helix	326-334	9
α-helix	339-347	9
α-helix	353-360	8

Chain D: 18 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	50	1	21
β-strand	53-58	6	21
β-strand	66-72	7	21
β-strand	78-85	8	21
α-helix	91-106	16
β-strand	112	1	22
α-helix	113-114	2
β-strand	115-120	6	21
β-strand	124-129	6	21
β-strand	135-136	2	22
α-helix	137-144	8
α-helix	149-168	20
β-strand	171-172	2	23
α-helix	178-180	3
β-strand	181-183	3	22
β-strand	189-191	3	22
β-strand	198-199	2	23
β-strand	201	1	24
β-strand	204	1	24
β-strand	206	1	25
β-strand	211	1	26
α-helix	213-215	3
α-helix	218-221	4
β-strand	226	1	25
α-helix	229-245	17
β-strand	247	1	27
α-helix	255-264	10
α-helix	268-270	3
α-helix	275-282	8
α-helix	293-294	2
α-helix	295-298	4
α-helix	302-305	4
α-helix	318-321	4
α-helix	326-334	9
α-helix	339-347	9
α-helix	353-361	9

Chains E, F, G and H: 0 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	949	1	6
β-strand	956	1	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine-protein kinase MARK2	A, B, C, D	protein	319	Homo sapiens	Q7KZI7 (AlphaFold model)
Cytotoxicity-associated immunodominant antigen	E, F, G, H	protein	125	Helicobacter pylori	P55980 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>3IEC_1 Serine/threonine-protein kinase MARK2 (chains A, B, C, D)
MADLHIGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIM
KVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVFDYLVAHGWMKEKEARAKFRQIVSAVQ
YCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCGSPPYAAPELFQGK
KYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKF
LILNPSKRGTLEQIMKDRWMNVGHEDDELKPYVEPLPDYKDPRRTELMVSMGYTREEIQD
SLVGQRYNEVMATYLLLGY

Sequence of entity 2 (E, F, G, H), FASTA

>3IEC_2 Cytotoxicity-associated immunodominant antigen (chains E, F, G, H)
GPVDNNNNNGLKNSTEPIYAKVNKKKTGQVASPEEPIYTQVAKKVNAKIDRLNQIASGLG
GVGQAAGFPLKRHDKVDDLSKVGLSASPEPIYATIDDLGGPFPLKRHDKVDDLSKVGRSR
NQELA

Primary citation

Helicobacter pylori CagA inhibits PAR1-MARK family kinases by mimicking host substrates. Nesic, D., Miller, M.C., Quinkert, Z.T. et al. Nat Struct Mol Biol (2010) 17:130-132. DOI 10.1038/nsmb.1705 · PubMed

Other PDB entries of the same protein (UniProt Q7KZI7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8TXY 2.1 Å, X-ray crystal structure of JRD-SIK1/2i-3 bound to a MARK2-SIK2 chimera
5EAK 2.8 Å, Optimization of Microtubule Affinity Regulating Kinase (MARK) Inhibitors with Improved…
5KZ7 3.2 Å, Mark2 complex with 7-[(1S)-1-(4-fluorophenyl)ethyl]-5,5-dimethyl-2-(3-pyridylamino)pyrrol…
5KZ8 3.21 Å, Mark2 complex with 7-[(1S)-1-(4-fluorophenyl)ethyl]-5,5-dimethyl-2-(3-pyridylamino)pyrrol…

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