4GS7: Interleukin-15 quaternary complex

Structure of the Interleukin-15 quaternary complex. Determined by X-ray diffraction at 2.35 Å resolution. Released 7 Nov 2012.

Method: X-ray diffraction
Resolution: 2.35 Å
Organism: Homo sapiens
Chains: 4
Atoms: 5,053
Mol. weight: 71.8 kDa
Ligands: NAG
Released: 7 Nov 2012

Explore 4GS7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4GS7 contains 22 α-helices and 44 β-strands across 4 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: 6 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	1-16	16
β-strand	25-27	3	1
α-helix	33-35	3
α-helix	36-54	19
α-helix	57-76	20
α-helix	88-90	3
β-strand	92-94	3	1
α-helix	96-111	16

Chain B: 6 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	7-12	6	2
β-strand	17-23	7	2
β-strand	33-39	7	3
β-strand	46-49	4	3
β-strand	51-52	2	2
β-strand	57-63	7	2
β-strand	78-86	9	3
β-strand	89-98	10	3
α-helix	100-102	3
β-strand	104	1	2
α-helix	106-109	4
β-strand	110-117	8	4
β-strand	122-127	6	4
α-helix	133-135	3
β-strand	139-146	8	5
α-helix	152-154	3
β-strand	158-160	3	5
β-strand	166-169	4	4
α-helix	172-173	2
β-strand	177-186	10	5
α-helix	194-200	7
β-strand	201-204	4	5

Chain C: 6 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	33-38	6
β-strand	39-43	5	6
β-strand	47-51	5	6
β-strand	64-69	6	7
β-strand	78-79	2	7
β-strand	83-86	4	6
β-strand	89-96	8	6
α-helix	97-99	3
β-strand	106-111	6	7
β-strand	119-124	6	7
α-helix	126-128	3
β-strand	130-131	2	6
α-helix	132-135	4
β-strand	136-144	9	8
β-strand	147-153	7	8
α-helix	158-160	3
β-strand	161-169	9	9
β-strand	176-180	5	9
β-strand	185-188	4	8
β-strand	197-205	9	9
α-helix	214-221	8
β-strand	222-224	3	9

Chain D: 4 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	2	1	10
α-helix	3-8	6
β-strand	12-13	2	11
β-strand	20	1	10
β-strand	24-26	3	12
β-strand	28-29	2	11
α-helix	30	1
β-strand	33-35	3	13
α-helix	36	1
β-strand	42-44	3	12
β-strand	45-48	4	14
β-strand	53-56	4	14
α-helix	57-59	3
β-strand	63-65	3	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Interleukin-15	A	protein	116	Homo sapiens	P40933 (AlphaFold model)
Interleukin-2 receptor subunit beta	B	protein	217	Homo sapiens	P14784 (AlphaFold model)
Cytokine receptor common subunit gamma	C	protein	203	Homo sapiens	P31785 (AlphaFold model)
Interleukin-15 receptor subunit alpha	D	protein	69	Homo sapiens	Q13261 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4GS7_1 Interleukin-15 (chains A)
MGNWVNVISDLKKIEDLIQSMHIDATLYTESDVHPSCKVTAMKCFLLELQVISLESGDAS
IHDTVENLIILANNSLSSNGNVTESGCKECEELEEKNIKEFLQSFVHIVQMFINTS

Sequence of entity 2 (B), FASTA

>4GS7_2 Interleukin-2 receptor subunit beta (chains B)
ADPAVQGTSQFTCFYNSRAQISCVWSQDGALQDTSCQVHAWPDRRRWQQTCELLPVSQAS
WACNLILGAPDSQKLTTVDIVTLRVLCREGVRWRVMAIQDFKPFENLRLMAPISLQVVHV
ETHRCNISWEISQASHYFERHLEFEARTLSPGHTWEEAPLLTLKQKQEWICLETLTPDTQ
YEFQVRVKPLQGEFTTWSPWSQPLAFRTKPAALGKDT

Sequence of entity 3 (C), FASTA

>4GS7_3 Cytokine receptor common subunit gamma (chains C)
ADPLPLPEVQCFVFNVEYMNCTWQSSSEPQPTNLTLHYWYKNSDNDKVQKCSHYLFSEEI
TSGCQLQKKEIHLYQTFVVQLQDPREPRRQATQMLKLQNLVIPWAPENLTLHKLSESQLE
LNWNNRFLNHCLEHLVQYRTDWDHSWTEQSVDYRHKFSLPSVDGQKRYTFRVRSRFNPLC
GSAQHWSEWSHPIHWGSNTSKEN

Sequence of entity 4 (D), FASTA

>4GS7_4 Interleukin-15 receptor subunit alpha (chains D)
MGITCPPPMSVEHADIWVKSYSLYSRERYICNSGFKRKAGTSSLTECVLNKATNVAHWTT
PSLKCIRDP

Ligands and cofactors

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

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

Primary citation

Mechanistic and structural insight into the functional dichotomy between IL-2 and IL-15. Ring, A.M., Lin, J.X., Feng, D. et al. Nat Immunol (2012) 13:1187-1195. DOI 10.1038/ni.2449 · PubMed

Other PDB entries of the same protein (UniProt P40933 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2Z3Q 1.85 Å, Crystal structure of the IL-15/IL-15Ra complex
2Z3R 2.0 Å, Crystal structure of the IL-15/IL-15Ra complex
2XQB 2.6 Å, Crystal Structure of anti-IL-15 Antibody in Complex with human IL-15

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