7A1K: FACTOR INHIBITING HIF-1 ALPHA

FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH ZN(II) AND 3-((9,9-dimethyl-9H-fluoren-2-yl)methyl)-2-oxoglutarate. Determined by X-ray diffraction at 1.99 Å resolution. Released 25 Aug 2021.

Method: X-ray diffraction
Resolution: 1.99 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,861
Mol. weight: 41.13 kDa
Ligands: QVZ, ZN
Released: 25 Aug 2021

Explore 7A1K in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7A1K contains 24 α-helices and 20 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: 24 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	16-17	2
β-strand	18	1	1
α-helix	19	1
α-helix	20-22	3
β-strand	25	1	1
α-helix	29-31	3
α-helix	33-34	2
β-strand	39-41	3	2
α-helix	42-43	2
β-strand	44-45	2	3
α-helix	50-57	8
β-strand	62-64	3	3
α-helix	71-75	5
α-helix	78-84	7
β-strand	90-95	6	3
β-strand	99	1	2
α-helix	105-109	5
β-strand	119-123	5	3
α-helix	125-137	13
β-strand	143-149	7	3
α-helix	156-163	8
α-helix	167-176	10
β-strand	182-190	9	3
β-strand	195-199	5	2
β-strand	204-211	8	3
β-strand	214-219	6	2
α-helix	221-223	3
α-helix	224-227	4
β-strand	229	1	4
α-helix	230-231	2
β-strand	239	1	2
β-strand	240	1	4
α-helix	253-257	5
β-strand	260-265	6	2
β-strand	270-273	4	3
β-strand	278-283	6	2
α-helix	284	1
β-strand	290-297	8	3
α-helix	298-303	6
α-helix	306-307	2
α-helix	310-311	2
α-helix	312-330	19
α-helix	333-335	3
α-helix	336-344	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Hypoxia-inducible factor 1-alpha inhibitor	A	protein	349	Homo sapiens	Q9NWT6 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>7A1K_1 Hypoxia-inducible factor 1-alpha inhibitor (chains A)
MAATAAEAVASGSGEPREEAGALGPAWDESQLRSYSFPTRPIPRLSQSDPRAEELIENEE
PVVLTDTNLVYPALKWDLEYLQENIGNGDFSVYSASTHKFLYYDEKKMANFQNFKPRSNR
EEMKFHEFVEKLQDIQQRGGEERLYLQQTLNDTVGRKIVMDFLGFNWNWINKQQGKRGWG
QLTSNLLLIGMEGNVTPAHYDEQQNFFAQIKGYKRCILFPPDQFECLYPYPVHHPCDRQS
QVDFDNPDYERFPNFQNVVGYETVVGPGDVLYIPMYWWHHIESLLNGGITITVNFWYKGA
PTPKRIEYPLKAHQKVAIMRNIEKMLGEALGNPQEVGPLLNTMIKGRYN

Ligands and cofactors

ID	Name	Formula	Copies
QVZ	3-((9,9-dimethyl-9H-fluoren-2-yl)methyl)-2-oxoglutarate	C21 H20 O5	1
ZN	Zinc ion	Zn	1

Water and common crystallization additives (SO4) are not listed.

Primary citation

2-Oxoglutarate derivatives can selectively enhance or inhibit the activity of human oxygenases. Nakashima, Y., Brewitz, L., Tumber, A. et al. Nat Commun (2021) 12:6478-6478. DOI 10.1038/s41467-021-26673-2 · PubMed

Other PDB entries of the same protein (UniProt Q9NWT6 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7A1Q 1.75 Å, FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH ZN(II), 3-(carboxycarbonyl)cyclopentane-1-c…
7A1P 1.76 Å, FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH ZN(II), 4-propyl-2-oxoglutarate, AND…
6H9J 1.83 Å, Factor Inhibiting HIF (FIH) in complex with zinc, NOG and TRPV3 (229-255)
6HC8 1.9 Å, Factor Inhibiting HIF (FIH) in complex with zinc, NOG and TRPA1 (313-339)
6HKP 1.9 Å, Factor Inhibiting HIF (FIH) in complex with zinc, NOG and ASPP2 (970-992)
7A1J 1.9 Å, FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH ZN(II) AND 3-(3-phenylpropyl)-2-oxoglutarate
6HL6 1.97 Å, Factor Inhibiting HIF (FIH) in complex with zinc, NOG and iASPP(670-693)
6HA6 1.98 Å, Factor Inhibiting HIF (FIH) in complex with zinc, NOG and TRPV3 (220-246)
6HL5 1.98 Å, Factor Inhibiting HIF (FIH) in complex with zinc, NOG and ASPP1(932-954)
7A1N 2.01 Å, FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH ZN(II), 3-methyl-2-oxoglutarate, AND…
7A1S 2.01 Å, FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH ZN(II), 3-methyl-2-oxoglutarate, AND…
8K73 2.02 Å, Factor-inhibiting hypoxia-inducible factor in complex with Zn(II) and…

Browse structure collections

About this viewer

MolViewer shows 7A1K directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.