6E2Q: Human JAK2 FERM/SH2

Structure of human JAK2 FERM/SH2 in complex with Erythropoietin Receptor. Determined by X-ray diffraction at 2.65 Å resolution. Released 8 Aug 2018.

Method: X-ray diffraction
Resolution: 2.65 Å
Organism: Homo sapiens
Chains: 8
Atoms: 16,599
Mol. weight: 258.98 kDa
Released: 8 Aug 2018

Explore 6E2Q in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6E2Q contains 83 α-helices and 121 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: 19 helices, 30 β-strands

Element	Residues	Length	Sheet
β-strand	38-43	6	1
β-strand	53-55	3	1
β-strand	60-63	4	2
α-helix	64-75	12
α-helix	82-84	3
β-strand	85-89	5	1
β-strand	95	1	1
α-helix	96-97	2
β-strand	101-104	4	2
β-strand	109-116	8	1
β-strand	125	1	3
β-strand	131-134	4	4
β-strand	141-142	2	4
α-helix	147-162	16
α-helix	172-193	22
α-helix	197-203	7
α-helix	206-209	4
α-helix	212-219	8
α-helix	223-240	18
β-strand	244	1	5
α-helix	247-261	15
α-helix	263-266	4
β-strand	268-273	6	6
β-strand	285-291	7	6
β-strand	295-300	6	6
α-helix	311-313	3
β-strand	315-318	4	6
α-helix	320-322	3
β-strand	323-330	8	6
β-strand	340-346	7	6
β-strand	352-356	5	6
α-helix	359-376	18
α-helix	385-387	3
α-helix	390-398	9
β-strand	401	1	7
α-helix	406-416	11
β-strand	422-427	6	7
β-strand	434-443	10	7
β-strand	446-456	11	7
β-strand	462-464	3	7
β-strand	465	1	8
β-strand	467	1	8
β-strand	471	1	7
α-helix	474-481	8
β-strand	485-488	4	9
β-strand	491-494	4	9
β-strand	497-498	2	7
α-helix	500-502	3
β-strand	511-513	3	4

Chain B: 18 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	39-43	5	10
β-strand	53-57	5	10
β-strand	60-63	4	11
α-helix	64-74	11
α-helix	82-84	3
β-strand	85-89	5	10
β-strand	95-96	2	10
β-strand	101-104	4	11
β-strand	110-116	7	10
β-strand	125	1	12
β-strand	131-134	4	13
β-strand	141-142	2	13
α-helix	147-162	16
α-helix	172-193	22
α-helix	197-203	7
α-helix	206-209	4
α-helix	212-218	7
α-helix	223-239	17
α-helix	240-242	3
β-strand	244	1	14
α-helix	247-261	15
α-helix	263-266	4
β-strand	268-273	6	15
α-helix	282-284	3
β-strand	285-291	7	15
β-strand	295-300	6	15
α-helix	311-313	3
β-strand	315-318	4	15
α-helix	320-322	3
β-strand	323-329	7	15
β-strand	340-346	7	15
β-strand	352-356	5	15
α-helix	359-376	18
α-helix	390-397	8
β-strand	401	1	16
α-helix	406-415	10
β-strand	422-427	6	16
β-strand	434-443	10	16
β-strand	446-456	11	16
β-strand	462-464	3	16
β-strand	471	1	16
α-helix	474-481	8
β-strand	485-488	4	17
β-strand	491-494	4	17
β-strand	497-498	2	16
β-strand	511-513	3	13

Chain C: 18 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	38-43	6	18
β-strand	53-57	5	18
β-strand	60-63	4	19
α-helix	64-74	11
α-helix	79-84	6
β-strand	85-89	5	18
β-strand	95	1	18
β-strand	101-104	4	19
β-strand	109-116	8	18
β-strand	125	1	20
β-strand	131-134	4	21
β-strand	141-142	2	21
α-helix	147-162	16
α-helix	172-192	21
α-helix	197-203	7
α-helix	206-209	4
α-helix	212-220	9
α-helix	223-237	15
α-helix	238-242	5
β-strand	244	1	22
α-helix	247-261	15
α-helix	263-266	4
β-strand	268-273	6	23
β-strand	285-291	7	23
β-strand	295-300	6	23
α-helix	311-313	3
β-strand	315-318	4	23
α-helix	320-322	3
β-strand	323-330	8	23
β-strand	340-346	7	23
β-strand	352-356	5	23
α-helix	359-376	18
α-helix	385-387	3
α-helix	390-397	8
β-strand	401	1	24
α-helix	406-416	11
β-strand	422-427	6	24
β-strand	434-440	7	24
β-strand	449-456	8	24
β-strand	462-464	3	24
β-strand	470-471	2	24
α-helix	474-482	9
β-strand	485-487	3	25
β-strand	492-494	3	25
β-strand	497-498	2	24
β-strand	511-513	3	21

Chain D: 17 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	39-43	5	26
β-strand	53-57	5	26
β-strand	60-63	4	27
α-helix	64-75	12
α-helix	79-84	6
β-strand	85-89	5	26
β-strand	95-96	2	26
β-strand	101-104	4	27
β-strand	110-116	7	26
β-strand	125	1	28
β-strand	131-134	4	29
β-strand	141-142	2	29
α-helix	147-162	16
α-helix	172-192	21
α-helix	197-203	7
α-helix	206-209	4
α-helix	212-220	9
α-helix	223-237	15
α-helix	239-242	4
β-strand	244	1	30
α-helix	247-261	15
α-helix	263-266	4
β-strand	267-273	7	31
β-strand	285-291	7	31
β-strand	295-300	6	31
α-helix	311-313	3
β-strand	315-318	4	31
β-strand	323-329	7	31
β-strand	340-346	7	31
α-helix	350-351	2
β-strand	352-356	5	31
α-helix	359-376	18
α-helix	390-397	8
β-strand	401	1	32
α-helix	406-414	9
β-strand	424-427	4	32
β-strand	434-438	5	32
β-strand	451-456	6	32
β-strand	462-464	3	32
β-strand	471	1	32
α-helix	474-480	7
β-strand	511-513	3	29

Chains M and P: 2 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	289-293	5
β-strand	303	1	22
α-helix	304-311	8
β-strand	314	1	20

Chain N: 4 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	289-293	5
β-strand	303	1	5
α-helix	304-312	9
β-strand	314	1	3
α-helix	319-322	4
α-helix	324-330	7
β-strand	332-333	2	9

Chain O: 3 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	289-293	5
β-strand	303	1	14
α-helix	304-312	9
β-strand	314	1	12
α-helix	325-330	6
β-strand	332-333	2	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tyrosine-protein kinase JAK2	A, B, C, D	protein	483	Homo sapiens	O60674 (AlphaFold model)
Erythropoietin receptor	M, N, O, P	protein	83	Homo sapiens	P19235 (AlphaFold model)

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

>6E2Q_1 Tyrosine-protein kinase JAK2 (chains A, B, C, D)
GSDPVLQVYLYHSLGKSEADYLTFPSGEYVAEEICIAASKACGITPVYHNMFALMSETER
IWYPPNHVFHIDESTRHNVLYRIRFYFPRWYCSGSNRAYRHGISRGAEAPLLDDFVMSYL
FAQWRHDFVHGWIKVPVTHETQEECLGMAVLDMMRIAKENDQTPLAIYNSISYKTFLPKC
IRAKIQDYHILTRKRIRYRFRRFIQQFSQCKATARNLKLKYLINLETLQSAFYTEKFEVK
EPGSGPSGEEIFATIIITGNGGIQWSRGKHKESETLTEQDLQLYCDFPNIIDVSIKQANQ
EGSNESRVVTIHKQDGKNLEIELSSLREALSFVSLIDGYYRLTADAHHYLCKEVAPPAVL
ENIQSNCHGPISMDFAISKLKKAGNQTGLYVLRCSPKDFNKYFLTFAVERENVIEYKHCL
ITKNENEEYNLSGTKKNFSSLKDLLNCYQMETVRSDNIIFQFTKCCPPKPKDKSNLLVFR
TGS

Sequence of entity 2 (M, N, O, P), FASTA

>6E2Q_2 Erythropoietin receptor (chains M, N, O, P)
GSGSGSGSGSGSGSSHRRALKQKIWPGIPSPESEFEGLFTTHKGNFQLWLYQNDGCLWWS
PCTPFTEDPPASLEVLSERCGNS

Primary citation

Receptor-mediated dimerization of JAK2 FERM domains is required for JAK2 activation. Ferrao, R.D., Wallweber, H., Lupardus, P.J. Elife (2018) 7. DOI 10.7554/eLife.38089 · PubMed

Other PDB entries of the same protein (UniProt O60674 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8BXH 1.3 Å, Crystal structure of JAK2 JH1 in complex with momelotinib
7LL4 1.31 Å, High-resolution crystal structure of human JAK2 kinase domain (JH1) bound to PN5-114.
3UGC 1.34 Å, Structural basis of Jak2 inhibition by the type II inhibtor NVP-BBT594
7REE 1.38 Å, High-resolution crystal structure of human JAK2 kinase domain (JH1) bound to YM2-059
8BA3 1.4 Å, Crystal structure of JAK2 JH2 in complex with Bemcentinib
8BX9 1.4 Å, Crystal structure of JAK2 JH1 in complex with ilginatinib
7TEU 1.45 Å, Crystal structure of JAK2 JH1 with type II inhibitor YLIU-04-105-1
9TM5 1.45 Å, Crystal structure of JAK2 JH1 in complex with AT9283
4IVA 1.5 Å, JAK2 kinase (JH1 domain) in complex with the inhibitor TRANS-4-[(8AS)-2-[(1R)-1-HYDROXYET…
7LL5 1.5 Å, High-resolution crystal structure of human JAK2 kinase domain (JH1) bound to PN5-150.
7RN6 1.5 Å, High-resolution crystal structure of human JAK2 kinase domain (JH1) bound to type-II…
8B8U 1.5 Å, Crystal structure of JAK2 JH2-V617F in complex with HTS-A3

Browse structure collections

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