7ZMZ: Engineered Interleukin 2

Engineered Interleukin 2 bound to CD25 receptor. Determined by X-ray diffraction at 3.2 Å resolution. Released 14 Dec 2022.

Method: X-ray diffraction
Resolution: 3.2 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,028
Mol. weight: 45.84 kDa
Released: 14 Dec 2022

Explore 7ZMZ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7ZMZ contains 14 α-helices and 23 β-strands across 2 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, 4 β-strands

Element	Residues	Length	Sheet
α-helix	5-28	24
α-helix	36-40	5
β-strand	44	1	1
β-strand	47	1	2
α-helix	53-55	3
α-helix	56-70	15
α-helix	82-94	13
β-strand	107	1	2
β-strand	112	1	1
α-helix	114-132	19

Chain D: 8 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	1	1
β-strand	2	1	3
α-helix	3	1
α-helix	6-9	4
β-strand	13-17	5	4
β-strand	20-21	2	5
β-strand	25-27	3	6
β-strand	30	1	7
α-helix	31	1
β-strand	35-36	2	8
α-helix	37	1
β-strand	43-46	4	6
β-strand	55-56	2	6
β-strand	61-62	2	8
β-strand	103-104	2	5
α-helix	107-109	3
β-strand	113	1	7
β-strand	119-120	2	6
β-strand	122	1	3
β-strand	126-131	6	4
α-helix	132	1
β-strand	136-137	2	9
β-strand	144-146	3	4
β-strand	147-150	4	10
β-strand	153-156	4	10
α-helix	157-159	3
β-strand	163-164	2	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Interleukin-2	A	protein	146	Homo sapiens	P60568 (AlphaFold model)
Interleukin-2 receptor subunit alpha	D	protein	258	Homo sapiens	P01589 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>7ZMZ_1 Interleukin-2 (chains A)
GSAPTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLHLMLSYGFYMPKKATELKHLQC
LEEELKPLEEVLNLAQSKFNHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFL
NRWITFCQSIISTLTAAAHHHHHHHH

Sequence of entity 2 (D), FASTA

>7ZMZ_2 Interleukin-2 receptor subunit alpha (chains D)
GAELCDDDPPEIPHATFKAMAYKEGTMLNCECKRGFRRIKSGSLYMLCTGNSSHSSWDNQ
CQCTSSATRNTTKQVTPQPEEQKERKTTEMQSPMQPVDQASLPGHCREPPPWENEATERI
YHFVVGQMVYYQCVQGYRALHRGPAESVCKMTHGKTRWTQPQLICTGEMETSQFPGEEKP
QASPEGRPESETSCLVTTTDFQIQTEMAATMETSIFTTEAAALEVLFQGPGAAGGGLNDI
FEAQKIEWHEHHHHHHHH

Primary citation

IL-2 is inactivated by the acidic pH environment of tumors enabling engineering of a pH-selective mutein. Gaggero, S., Martinez-Fabregas, J., Cozzani, A. et al. Sci Immunol (2022) 7:eade5686-eade5686. DOI 10.1126/sciimmunol.ade5686 · PubMed

Other PDB entries of the same protein (UniProt P60568 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8SOZ 1.64 Å, Structure of the complex formed by human interleukin-2 and scFv 602
8SOW 1.71 Å, Structure of the complex formed by human interleukin-2 and scFv F10
7M2G 1.79 Å, INTERLEUKIN-2 (human) mutant P65K, C125S
4NEJ 1.92 Å, Small molecular fragment bound to crystal contact interface of Interleukin-2
4NEM 1.93 Å, Small molecular fragment bound to crystal contact interface of Interleukin-2
1M48 1.95 Å, Crystal Structure of Human IL-2 Complexed with (R)-N-[2-[1-(Aminoiminomethyl)-3-piperidin…
5LQB 1.95 Å, Complex structure of human IL2 mutant, Proleukin, with Fab fragment of NARA1 antibody
1M47 1.99 Å, Crystal Structure of Human Interleukin-2
1M49 2.0 Å, Crystal Structure of Human Interleukin-2 Complexed with SP-1985
1M4B 2.15 Å, Crystal Structure of Human Interleukin-2 K43C Covalently Modified at C43 with…
1M4A 2.18 Å, Crystal Structure of Human Interleukin-2 Y31C Covalently Modified at C31 with…
1NBP 2.2 Å, Crystal Structure Of Human Interleukin-2 Y31C Covalently Modified At C31 With…

Browse structure collections

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