8ENT: Interleukin-21

Interleukin-21 signaling complex with IL-21R and IL-2Rg. Determined by X-ray diffraction at 2.83 Å resolution. Released 28 Jun 2023.

Method: X-ray diffraction
Resolution: 2.83 Å
Organism: Homo sapiens
Chains: 11
Atoms: 15,852
Mol. weight: 255.81 kDa
Ligands: NAG
Released: 28 Jun 2023

Explore 8ENT in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8ENT contains 90 α-helices and 139 β-strands across 11 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: 9 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	5-22	18
α-helix	24-26	3
β-strand	27	1	1
β-strand	32-33	2	2
α-helix	43-52	10
β-strand	57	1	1
α-helix	64-74	11
α-helix	77-78	2
α-helix	84-86	3
α-helix	87-89	3
α-helix	94-95	2
β-strand	101-102	2	2
α-helix	104-126	23

Chains B and H: 10 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	3
β-strand	13-19	7	3
α-helix	25-26	2
β-strand	27-32	6	4
β-strand	45-48	4	4
β-strand	49-53	5	3
β-strand	57-63	7	3
α-helix	66-68	3
β-strand	74-80	7	4
β-strand	87-94	8	4
α-helix	95-97	3
β-strand	99	1	3
α-helix	101-104	4
β-strand	105-111	7	5
β-strand	115-120	6	5
α-helix	122-124	3
α-helix	126-131	6
β-strand	135-143	9	6
β-strand	147	1	7
α-helix	151-152	2
β-strand	153-157	5	6
β-strand	163-166	4	5
α-helix	168-170	3
β-strand	176-185	10	6
β-strand	193	1	3
α-helix	195-201	7
β-strand	202-205	4	6
α-helix	206-207	2

Chain C: 6 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	33-38	6
β-strand	39	1	8
β-strand	42-43	2	8
β-strand	47-51	5	8
β-strand	64-69	6	9
β-strand	78-79	2	9
β-strand	83-85	3	8
β-strand	90-95	6	8
α-helix	97-99	3
β-strand	105-111	7	9
β-strand	119-125	7	9
α-helix	126-129	4
β-strand	130-131	2	8
α-helix	132-135	4
β-strand	136-144	9	10
β-strand	147-153	7	10
α-helix	158-160	3
β-strand	161-169	9	11
β-strand	176-180	5	11
β-strand	185-188	4	10
β-strand	197-205	9	11
α-helix	214-219	6
β-strand	222-224	3	11

Chain D: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	5-22	18
α-helix	24-26	3
β-strand	27	1	12
β-strand	32-33	2	13
α-helix	38-39	2
α-helix	43-52	10
β-strand	57	1	12
α-helix	64-74	11
α-helix	77-80	4
α-helix	94-95	2
β-strand	101-102	2	13
α-helix	104-124	21

Chains E and K: 10 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	14
β-strand	13-19	7	14
α-helix	25-26	2
β-strand	27-32	6	15
β-strand	45-48	4	15
β-strand	49-53	5	14
β-strand	57-63	7	14
α-helix	66-68	3
β-strand	74-80	7	15
β-strand	87-94	8	15
α-helix	95-97	3
β-strand	99	1	14
α-helix	101-104	4
β-strand	105-111	7	16
β-strand	115-120	6	16
α-helix	122-124	3
α-helix	126-131	6
β-strand	135-143	9	17
β-strand	147	1	18
α-helix	150-152	3
β-strand	153-157	5	17
β-strand	163-166	4	16
α-helix	168-170	3
β-strand	176-185	10	17
β-strand	193	1	14
α-helix	195-201	7
β-strand	202-205	4	17
α-helix	206-207	2

Chain F: 5 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	33-38	6
β-strand	39	1	19
β-strand	42-43	2	19
β-strand	47-51	5	19
β-strand	64-69	6	20
β-strand	78-79	2	20
β-strand	83-86	4	19
β-strand	89-95	7	19
β-strand	105-111	7	20
β-strand	119-125	7	20
α-helix	127-129	3
β-strand	130-131	2	19
α-helix	132-135	4
β-strand	136-144	9	21
β-strand	147-153	7	21
α-helix	158-160	3
β-strand	162-169	8	22
β-strand	176-180	5	22
β-strand	185-188	4	21
β-strand	197-204	8	22
α-helix	214-219	6
β-strand	222-224	3	22

Chain G: 9 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	5-22	18
α-helix	24-26	3
β-strand	27	1	23
β-strand	32-33	2	24
α-helix	43-51	9
β-strand	57	1	23
α-helix	64-74	11
α-helix	77-78	2
α-helix	82-85	4
α-helix	94-95	2
α-helix	100	1
β-strand	101-102	2	24
α-helix	104-126	23

Chain I: 5 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	33-38	6
β-strand	39	1	29
β-strand	42-43	2	29
β-strand	47-51	5	29
β-strand	64-69	6	30
β-strand	78-79	2	30
β-strand	83-86	4	29
β-strand	89-95	7	29
α-helix	97-99	3
β-strand	106-112	7	30
β-strand	115-124	10	30
β-strand	130-131	2	29
α-helix	132-135	4
β-strand	136-144	9	31
β-strand	147-153	7	31
α-helix	158-160	3
β-strand	161-169	9	32
β-strand	176-180	5	32
β-strand	185-188	4	31
β-strand	196-205	10	32
α-helix	214-219	6
β-strand	222-225	4	32

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
Interleukin-21	A, D, G, J	protein	144	Homo sapiens	Q9HBE4 (AlphaFold model)
Interleukin-21 receptor	B, E, H, K	protein	237	Homo sapiens	Q9HBE5 (AlphaFold model)
Cytokine receptor common subunit gamma	C, F, I	protein	207	Homo sapiens	P31785 (AlphaFold model)

Sequence of entity 1 (A, D, G, J), FASTA

>8ENT_1 Interleukin-21 (chains A, D, G, J)
QGQDRHMIRMRQLIDIVDQLKNYVNDLVPEFLPAPEDVETNCEWSAFSCFQKAQLKSANT
GNNERIIQVSIKKLKRKPPSTNAGRRQKHRLTCPSCDSYEKKPPKEFLERFKSLLQKMIH
QHLSSRTHGSEDSGAPGSHHHHHH

Sequence of entity 2 (B, E, H, K), FASTA

>8ENT_2 Interleukin-21 receptor (chains B, E, H, K)
CPDLVCYTDYLQTVICILEMWNLHPSTLTLTWQDQYEELKDEATSCSLHRSAHNATHATY
TCHMDVFHFMADDIFSVQITDQSGQYSQECGSFLLAESIKPAPPFDVTVTFSGQYQISWR
SDYEDPAFYMLKGKLQYELQYRNRGDPWAVSPRRKLISVDSRSVSLLPLEFRKDSSYELQ
VRAGPMPGSSYQGTWSEWSDPVIFQTQSEEKAASGRGLNDIFEAQKIEWHEHHHHHH

Sequence of entity 3 (C, F, I), FASTA

>8ENT_3 Cytokine receptor common subunit gamma (chains C, F, I)
PLPLPEVQCFVFNVEYMNCTWQSSSEPQPTNLTLHYWYKNSDNDKVQKCSHYLFSEEITS
GCQLQKKEIHLYQTFVVQLQDPREPRRQATQMLKLQNLVIPWAPENLTLHKLSESQLELN
WNNRFLNHCLEHLVQYRTDWDHSWTEQSVDYRHKFSLPSVDGQKRYTFRVRSRFNPLCGS
AQHWSEWSHPIHWGSNTSKENHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	7

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

Primary citation

A structural blueprint for interleukin-21 signal modulation. Abhiraman, G.C., Bruun, T.U.J., Caveney, N.A. et al. Cell Rep (2023) 42:112657-112657. DOI 10.1016/j.celrep.2023.112657 · PubMed

Other PDB entries of the same protein (UniProt Q9HBE4 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3TGX 2.8 Å, IL-21:IL21R complex
2OQP Solution structure of human interleukin-21

Browse structure collections

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