3QB7: Interleukin-4 mutant RGA

Interleukin-4 mutant RGA bound to cytokine receptor common gamma. Determined by X-ray diffraction at 3.25 Å resolution. Released 25 Apr 2012.

Method: X-ray diffraction
Resolution: 3.25 Å
Organism: Homo sapiens
Chains: 4
Atoms: 5,337
Mol. weight: 80.63 kDa
Ligands: NAG
Released: 25 Apr 2012

Explore 3QB7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3QB7 contains 19 α-helices and 37 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: 5 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	5-19	15
α-helix	24-26	3
β-strand	28-29	2	1
α-helix	41-59	19
α-helix	70-94	25
β-strand	107-108	2	1
α-helix	109-126	18

Chain B: 4 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	5-18	14
β-strand	28-30	3	2
α-helix	41-58	18
α-helix	70-94	25
β-strand	106-108	3	2
α-helix	109-126	18

Chain C: 4 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	38-43	6	3
β-strand	47-52	6	3
β-strand	64-69	6	4
β-strand	78-79	2	4
β-strand	83-86	4	3
β-strand	89-95	7	3
α-helix	97-99	3
β-strand	106-111	6	4
β-strand	119-124	6	4
β-strand	130-131	2	3
α-helix	132-135	4
β-strand	136-142	7	5
β-strand	148-153	6	5
α-helix	158-160	3
β-strand	162-168	7	6
β-strand	176-180	5	6
β-strand	186-188	3	5
β-strand	197-204	8	6
α-helix	214-218	5
β-strand	222-224	3	6

Chain D: 6 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	35-37	3
β-strand	38-43	6	7
β-strand	47-52	6	7
β-strand	64-69	6	8
β-strand	78-79	2	8
β-strand	83-85	3	7
β-strand	90-96	7	7
α-helix	97-99	3
β-strand	106-111	6	8
β-strand	119-124	6	8
α-helix	126-128	3
β-strand	130	1	7
α-helix	132-135	4
β-strand	136-141	6	9
β-strand	149-153	5	9
β-strand	161-168	8	10
β-strand	176-180	5	10
β-strand	185-187	3	9
β-strand	197-205	9	10
α-helix	214	1
β-strand	215	1	10
α-helix	216-221	6
β-strand	222-224	3	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Interleukin 4	A, B	protein	132	Homo sapiens	P05112 (AlphaFold model)
Cytokine receptor common subunit gamma	C, D	protein	203	Homo sapiens	P31785 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3QB7_1 Interleukin 4 (chains A, B)
ADPHKCDITLQEIIKTLNSLTEQKTLCTELTVTDIFAASKNTTEKETFCRAATVLRQFYS
HHEKDTRCLGATAQQFHRHKQLIRFLKRLDRNLWGLAGLNSCPVKEANQSTLENFLERLR
VIMQSKWFKCGA

Sequence of entity 2 (C, D), FASTA

>3QB7_2 Cytokine receptor common subunit gamma (chains C, D)
ADPLPLPEVQCFVFNVEYMNCTWQSSSEPQPTNLTLHYWYKNSDNDKVQKCSHYLFSEEI
TSGCQLQKKEIHLYQTFVVQLQDPREPRRQATQMLKLQNLVIPWAPENLTLHKLSESQLE
LNWNNRFLNHCLEHLVQYRTDWDHSWTEQSVDYRHKFSLPSVDGQKRYTFRVRSRFNPLC
GSAQHWSEWSHPIHWGSNTSKEN

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 (SO4) are not listed.

Primary citation

Redirecting cell-type specific cytokine responses with engineered interleukin-4 superkines. Junttila, I.S., Creusot, R.J., Moraga, I. et al. Nat Chem Biol (2012) 8:990-998. DOI 10.1038/nchembio.1096 · PubMed

Other PDB entries of the same protein (UniProt P05112 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2D48 1.65 Å, Crystal structure of the Interleukin-4 variant T13D
2B8X 1.7 Å, Crystal structure of the interleukin-4 variant F82D
2B8U 1.8 Å, Crystal structure of wildtype human Interleukin-4
2B8Y 1.8 Å, Crystal structure of the interleukin-4 variant T13DF82D
2B91 2.0 Å, Crystal structure of the interleukin-4 variant F82DR85A
4YDY 2.0 Å, Crystal structure of darpin 44C12V5 in complex with human il-4
1HZI 2.05 Å, Interleukin-4 mutant E9A
2B90 2.1 Å, Crystal structure of the interleukin-4 variant T13DR85A
1RCB 2.25 Å, Crystal structure of human recombinant interleukin-4 at 2.25 Å resolution
1IAR 2.3 Å, Interleukin-4 / receptor alpha chain complex
2INT 2.35 Å, Crystal structure of recombinant human interleukin-4
2B8Z 2.5 Å, Crystal structure of the interleukin-4 variant R85A

Browse structure collections

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