4GL9: Inhibitory protein SOCS3

Crystal structure of inhibitory protein SOCS3 in complex with JAK2 kinase domain and fragment of GP130 intracellular domain. Determined by X-ray diffraction at 3.9 Å resolution. Released 6 Mar 2013.

Method: X-ray diffraction
Resolution: 3.9 Å
Organism: Mus musculus
Chains: 12
Atoms: 13,682
Mol. weight: 210.77 kDa
Ligands: IZA, PO4
Released: 6 Mar 2013

Explore 4GL9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4GL9 contains 88 α-helices and 108 β-strands across 12 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: 15 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	849-858	10	1
β-strand	861-868	8	1
α-helix	876-877	2
β-strand	878-884	7	1
α-helix	889-903	15
β-strand	910	1	2
α-helix	911-912	2
β-strand	913-918	6	1
β-strand	925-930	6	1
β-strand	936	1	2
α-helix	937-943	7
α-helix	950-969	20
β-strand	972-973	2	3
α-helix	979-981	3
β-strand	982-986	5	2
β-strand	989-992	4	2
β-strand	999-1000	2	3
α-helix	1001-1002	2
β-strand	1008-1009	2	4
β-strand	1015	1	5
α-helix	1023-1027	5
β-strand	1030-1031	2	4
α-helix	1034-1049	16
α-helix	1057-1065	9
α-helix	1073-1083	11
α-helix	1088-1091	4
α-helix	1096-1105	10
α-helix	1114-1115	2
α-helix	1116-1129	14

Chain B: 15 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	849-858	10	6
β-strand	861-868	8	6
α-helix	876	1
β-strand	877-884	8	6
α-helix	889-903	15
β-strand	910	1	7
α-helix	911-912	2
β-strand	913-918	6	6
β-strand	925-930	6	6
β-strand	936	1	7
α-helix	937-943	7
α-helix	950-969	20
β-strand	972-973	2	8
α-helix	979-981	3
β-strand	982-986	5	7
β-strand	989-992	4	7
β-strand	999-1000	2	8
α-helix	1001-1002	2
β-strand	1008-1009	2	9
β-strand	1015	1	10
α-helix	1023-1027	5
β-strand	1030-1031	2	9
α-helix	1034-1049	16
α-helix	1057-1065	9
α-helix	1073-1083	11
α-helix	1088-1091	4
α-helix	1096-1105	10
α-helix	1114-1115	2
α-helix	1116-1129	14

Chain C: 15 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	849-858	10	13
β-strand	861-868	8	13
α-helix	876	1
β-strand	877-884	8	13
α-helix	889-903	15
β-strand	910	1	14
α-helix	911-912	2
β-strand	913-918	6	13
β-strand	925-930	6	13
β-strand	936	1	14
α-helix	937-943	7
α-helix	950-969	20
β-strand	972-973	2	15
α-helix	979-981	3
β-strand	982-986	5	14
β-strand	989-992	4	14
β-strand	999-1000	2	15
α-helix	1001-1002	2
β-strand	1008-1009	2	16
β-strand	1015	1	17
α-helix	1023-1027	5
β-strand	1030-1031	2	16
α-helix	1034-1049	16
α-helix	1057-1065	9
α-helix	1073-1083	11
α-helix	1088-1091	4
α-helix	1096-1105	10
α-helix	1114-1115	2
α-helix	1116-1127	12

Chain D: 15 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	849-858	10	24
β-strand	861-868	8	24
α-helix	877	1
β-strand	878-884	7	24
α-helix	889-903	15
β-strand	910	1	25
α-helix	911-912	2
β-strand	913-918	6	24
β-strand	925-930	6	24
β-strand	936	1	25
α-helix	937-943	7
α-helix	950-969	20
β-strand	972-973	2	26
α-helix	979-981	3
β-strand	982-986	5	25
β-strand	989-992	4	25
β-strand	999-1000	2	26
α-helix	1001-1002	2
β-strand	1008-1009	2	27
β-strand	1015	1	28
α-helix	1023-1027	5
β-strand	1030-1031	2	27
α-helix	1034-1049	16
α-helix	1057-1065	9
α-helix	1073-1083	11
α-helix	1088-1091	4
α-helix	1096-1105	10
α-helix	1114-1115	2
α-helix	1116-1127	12

Chains E and F: 7 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	23	1	5
α-helix	24-25	2
α-helix	28-44	17
β-strand	47-48	2	18
α-helix	53-59	7
β-strand	67-72	6	18
β-strand	80-85	6	18
β-strand	90-98	9	18
β-strand	101-104	4	18
α-helix	105	1
β-strand	106	1	19
α-helix	107	1
α-helix	113-115	3
β-strand	117	1	18
α-helix	120-127	8
β-strand	143-144	2	19
β-strand	151-152	2	19
β-strand	157-158	2	18

Chain G: 7 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	23	1	17
α-helix	24-25	2
α-helix	28-44	17
β-strand	47-48	2	11
α-helix	53-59	7
β-strand	67-72	6	11
β-strand	80-85	6	11
β-strand	90-98	9	11
β-strand	101-104	4	11
α-helix	105	1
β-strand	106	1	12
α-helix	107	1
α-helix	113-115	3
β-strand	117	1	11
α-helix	120-128	9
β-strand	143-144	2	12
β-strand	151-152	2	12
β-strand	157-158	2	11

Chain H: 7 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	23	1	10
α-helix	24-25	2
α-helix	28-44	17
β-strand	47-48	2	22
α-helix	53-59	7
β-strand	67-72	6	22
β-strand	80-85	6	22
β-strand	90-97	8	22
β-strand	102-104	3	22
α-helix	105	1
β-strand	106	1	23
α-helix	107	1
α-helix	113-115	3
β-strand	117	1	22
α-helix	120-128	9
β-strand	143-144	2	23
β-strand	151-152	2	23
β-strand	157-158	2	22

Chains I, J and K: 0 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	757	1	11
β-strand	760-761	2	12

1 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tyrosine-protein kinase	A, B, C, D	protein	297	Mus musculus	Q62120 (AlphaFold model)
Interleukin-6 receptor subunit beta	I, J, K, L	protein	15	Mus musculus	Q00560 (AlphaFold model)
Suppressor of cytokine signaling 3,Suppressor of cytokine signaling 3,Suppressor of cytokine…	E, F, G, H	protein	143	Mus musculus	O35718 (AlphaFold model)

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

>4GL9_1 Tyrosine-protein kinase (chains A, B, C, D)
FEDRDPTQFEERHLKFLQQLGKGNFGSVEMCRYDPLQDNTGEVVAVKKLQHSTEEHLRDF
EREIEILKSLQHDNIVKYKGVCYSAGRRNLRLIMEYLPYGSLRDYLQKHKERIDHKKLLQ
YTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQDKEYYKVKEPGE
SPIFWYAPESLTESKFSVASDVWSFGVVLYELFTYIEKSKSPPVEFMRMIGNDKQGQMIV
FHLIELLKSNGRLPRPEGCPDEIYVIMTECWNNNVSQRPSFRDLSLRVDQIRDSIAA

Sequence of entity 2 (I, J, K, L), FASTA

>4GL9_2 Interleukin-6 receptor subunit beta (chains I, J, K, L)
STASTVEYSTVVHSG

Sequence of entity 3 (E, F, G, H), FASTA

>4GL9_3 Suppressor of cytokine signaling 3,Suppressor of cytokine signaling 3,Suppressor of cytokine signaling 3,Suppressor of cytokine signaling 3 (chains E, F, G, H)
QGAHDLKTFSSKSEYQLVVNAVRKLQESGFYWSAVTGGEANLLLSAEPAGTFLIRDSSDQ
RHFFTLSVKTQSGTKNLRIQCEGGSFSLQSDPRSTQPVPRFDCVLKLVHHYMGSGSGSGS
RAYYIYSGGEKIPLVLSRPLSSN

Ligands and cofactors

ID	Name	Formula	Copies
IZA	2-tert-butyl-9-fluoro-3,6-dihydro-7H-benz[h]-IMIDAZ[4,5-f]isoquinoline-7-one	C18 H16 F N3 O	4
PO4	Phosphate ion	O4 P	1

Primary citation

SOCS3 binds specific receptor-JAK complexes to control cytokine signaling by direct kinase inhibition. Kershaw, N.J., Murphy, J.M., Liau, N.P. et al. Nat Struct Mol Biol (2013) 20:469-476. DOI 10.1038/nsmb.2519 · PubMed

Other PDB entries of the same protein (UniProt Q62120 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2HDX 2.35 Å, Crystal structure of the Src homology-2 domain of SH2-B in complex with Jak2 pTyr813…

Browse structure collections

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