4H6J: Hypoxia inducible factor 1-alpha

Identification of Cys 255 in HIF-1 as a novel site for development of covalent inhibitors of HIF-1 /ARNT PasB domain protein-protein interaction. Determined by X-ray diffraction at 1.52 Å resolution. Released 5 Dec 2012.

Method: X-ray diffraction
Resolution: 1.52 Å
Organism: Homo sapiens
Chains: 2
Atoms: 1,937
Mol. weight: 26.69 kDa
Released: 5 Dec 2012

Explore 4H6J in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4H6J contains 10 α-helices and 17 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: 4 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	241-246	6	1
β-strand	251	1	2
β-strand	252-255	4	1
α-helix	258-263	6
α-helix	267-270	4
β-strand	274	1	2
α-helix	275-277	3
β-strand	279	1	1
α-helix	284-297	14
β-strand	299-301	3	1
β-strand	305-308	4	1
β-strand	314-325	12	1
β-strand	332-341	10	1

Chain B: 6 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	359-361	3
β-strand	362-367	6	3
β-strand	372	1	4
β-strand	373-376	4	3
α-helix	380-384	5
α-helix	388-390	3
β-strand	395	1	4
α-helix	396-399	4
β-strand	400	1	3
α-helix	405-417	13
β-strand	423-430	8	3
β-strand	436-446	11	3
α-helix	453-455	3
β-strand	456-463	8	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Hypoxia inducible factor 1-alpha	A	protein	113	Homo sapiens	Q16665 (AlphaFold model)
Aryl hydrocarbon nuclear translocator	B	protein	116	Homo sapiens	P27540 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4H6J_1 HYPOXIA INDUCIBLE FACTOR 1-ALPHA (chains A)
GSDSKTFLSEHSLDMKFSYCDERITELMGYEPEELLGRSIYEYYHALDSDHLTKTHHDMF
TKGQVTTGQYRMLAKRGGYVWVETQATVIYNTKNSQPQCIVCVNYVVSGIIQH

Sequence of entity 2 (B), FASTA

>4H6J_2 ARYL HYDROCARBON NUCLEAR TRANSLOCATOR (chains B)
GSVCQPTRFISRHNIEGIFTFVDHRCVATVGYQPQELLGKNIVEFCHPEDQQLLRDSFQQ
VVKLKGQVLSVMFRFRSKNQEWLWMRTSSFTFQNPYSDEIEYIICTNTNVKNSSQE

Primary citation

Identification of Cys255 in HIF-1 alpha as a novel site for development of covalent inhibitors of HIF-1 alpha /ARNT PasB domain protein-protein interaction. Cardoso, R., Love, R., Nilsson, C.L. et al. Protein Sci (2012) 21:1885-1896. DOI 10.1002/pro.2172 · PubMed

Other PDB entries of the same protein (UniProt Q16665 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4AJY 1.73 Å, von Hippel-Lindau protein-ElonginB-ElonginC complex, bound to Hif1- alpha peptide
6GMR 1.75 Å, pVHL:EloB:EloC in complex with (4-(1H-pyrrol-1-yl)phenyl)methanol
8HE0 1.8 Å, Crystal structure of importin-alpha1 bound to the HIF-1alpha nuclear localization signal…
5L9V 1.83 Å, HIF prolyl hydroxylase 2 (PHD2-R281C/P317C) cross-linked to HIF-1alpha NODD-L397C/D412C…
6GFX 1.83 Å, pVHL:EloB:EloC in complex with modified HIF-1a CODD peptide containing…
1LM8 1.85 Å, Structure of a HIF-1a-pVHL-ElonginB-ElonginC Complex
8HE3 1.9 Å, Crystal structure of importin-alpha1 bound to the HIF-1alpha nuclear localization signal…
5L9B 1.95 Å, Hif prolyl hydroxylase 2 (PHD2/ EGLN1) in complex with 2-oxoglutarate (2OG) and…
1LQB 2.0 Å, Crystal structure of a hydroxylated HIF-1 alpha peptide bound to the…
3HQR 2.0 Å, PHD2:Mn:NOG:HIF1-alpha substrate complex
7QGS 2.0 Å, Crystal structure of p300 CH1 domain in complex with CITIF (a CITED2-HIF-1alpha hybrid)
7LVS 2.02 Å, The CBP TAZ1 Domain in Complex with a CITED2-HIF-1-Alpha Fusion Peptide

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