1F42: The P40 domain of human interleukin-12

Name: PDB 1F42: The P40 domain of human interleukin-12
Published: 2001-06-13
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: cytokine

The P40 domain of human interleukin-12. Determined by X-ray diffraction at 2.5 Å resolution. Released 13 Jun 2001.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,456
Mol. weight: 35.72 kDa
Ligands: MNB
Released: 13 Jun 2001

Explore 1F42 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1F42 contains 6 α-helices and 27 β-strands across 1 chain. 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, 27 β-strands

Element	Residues	Length	Sheet
β-strand	2-5	4	1
β-strand	8-14	7	1
β-strand	22-27	6	2
β-strand	37-40	4	1
β-strand	48-49	2	1
β-strand	52-57	6	2
α-helix	60-62	3
β-strand	64-70	7	1
β-strand	73-86	14	1
β-strand	89-90	2	1
β-strand	95	1	1
α-helix	96-97	2
β-strand	108-110	3	1
β-strand	111	1	3
β-strand	117-124	8	1
β-strand	130-138	9	1
β-strand	146-148	3	1
β-strand	152-159	8	1
β-strand	162-173	12	1
α-helix	181-182	2
β-strand	186-194	9	1
β-strand	197-205	9	1
α-helix	207-210	4
β-strand	211	1	3
α-helix	213-216	4
β-strand	217-223	7	4
β-strand	229-235	7	4
β-strand	249-256	8	5
β-strand	267-269	3	5
β-strand	273-277	5	4
β-strand	283-290	8	5
α-helix	296-300	5
β-strand	301-304	4	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Interleukin-12 beta chain	A	protein	306	Homo sapiens	P29460 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1F42_1 INTERLEUKIN-12 BETA CHAIN (chains A)
IWELKKDVYVVELDWYPDAPGEMVVLTCDTPEEDGITWTLDQSSEVLGSGKTLTIQVKEF
GDAGQYTCHKGGEVLSHSLLLLHKKEDGIWSTDILKDQKEPKNKTFLRCEAKNYSGRFTC
WWLTTISTDLTFSVKSSRGSSDPQGVTCGAATLSAERVRGDNKEYEYSVECQEDSACPAA
EESLPIEVMVDAVHKLKYENYTSSFFIRDIIKPDPPKNLQLKPLKNSRQVEVSWEYPDTW
STPHSYFSLTFCVQVQGKSKREKKDRVFTDKTSATVICRKNASISVRAQDRYYSSSWSEW
ASVPCS

Ligands and cofactors

ID	Name	Formula	Copies
MNB	5-mercapto-2-nitro-benzoic acid	C7 H5 N O4 S	2

Primary citation

Charged residues dominate a unique interlocking topography in the heterodimeric cytokine interleukin-12. Yoon, C., Johnston, S.C., Tang, J. et al. EMBO J (2000) 19:3530-3541. DOI 10.1093/emboj/19.14.3530 · PubMed

Other PDB entries of the same protein (UniProt P29460 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5MJ3 1.74 Å, Interleukin-23 complex with an antagonistic alphabody, crystal form 1
3D85 1.9 Å, Crystal structure of IL-23 in complex with neutralizing FAB
8CR8 2.0 Å, human Interleukin-23
3DUH 2.3 Å, Structure of Interleukin-23
8UUI 2.43 Å, X-ray structure of Interleukin-23 in complex with peptide 23-446
5MXA 2.5 Å, Structure of unbound Interleukin-23
4GRW 2.55 Å, Structure of a complex of human IL-23 with 3 Nanobodies (Llama vHHs)
6UIB 2.74 Å, Crystal structure of IL23 bound to peptide 23-652
1F45 2.8 Å, Human interleukin-12
5MZV 2.8 Å, IL-23:IL-23R:Nb22E11 complex
3D87 2.9 Å, Crystal structure of Interleukin-23
3HMX 3.0 Å, Crystal structure of ustekinumab FAB/IL-12 complex

Browse structure collections

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