1H2K: Factor Inhibiting HIF-1 alpha

Factor Inhibiting HIF-1 alpha in complex with HIF-1 alpha fragment peptide. Determined by X-ray diffraction at 2.15 Å resolution. Released 28 Nov 2002.

Method: X-ray diffraction
Resolution: 2.15 Å
Organism: HOMO SAPIENS
Chains: 2
Atoms: 3,090
Mol. weight: 45.23 kDa
Ligands: OGA, FE2
Released: 28 Nov 2002

Explore 1H2K in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1H2K contains 22 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: 21 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	16-17	2
β-strand	18-19	2	1
β-strand	24-25	2	1
α-helix	29-31	3
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	105-111	7
β-strand	118-123	6	3
α-helix	125-137	13
β-strand	143-149	7	3
α-helix	156-163	8
α-helix	167-177	11
β-strand	182-184	3	3
β-strand	186-190	5	3
β-strand	195-199	5	2
β-strand	203-211	9	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	290-298	9	3
α-helix	299-302	4
α-helix	308	1
α-helix	310-311	2
α-helix	312-330	19
α-helix	333-335	3
α-helix	336-344	9

Chain S: 1 helix, 2 β-strands

Element	Residues	Length	Sheet
β-strand	802	1	5
β-strand	804	1	5
α-helix	815-822	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Factor inhibiting HIF1	A	protein	349	HOMO SAPIENS	Q9NWT6 (AlphaFold model)
Hypoxia-inducible factor 1 alpha	S	protein	41	HOMO SAPIENS	Q16665 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1H2K_1 FACTOR INHIBITING HIF1 (chains A)
MAATAAEAVASGSGEPREEAGALGPAWDESQLRSYSFPTRPIPRLSQSDPRAEELIENEE
PVVLTDTNLVYPALKWDLEYLQENIGNGDFSVYSASTHKFLYYDEKKMANFQNFKPRSNR
EEMKFHEFVEKLQDIQQRGGEERLYLQQTLNDTVGRKIVMDFLGFNWNWINKQQGKRGWG
QLTSNLLLIGMEGNVTPAHYDEQQNFFAQIKGYKRCILFPPDQFECLYPYPVHHPCDRQS
QVDFDNPDYERFPNFQNVVGYETVVGPGDVLYIPMYWWHHIESLLNGGITITVNFWYKGA
PTPKRIEYPLKAHQKVAIMRNIEKMLGEALGNPQEVGPLLNTMIKGRYN

Sequence of entity 2 (S), FASTA

>1H2K_2 HYPOXIA-INDUCIBLE FACTOR 1 ALPHA (chains S)
SMDESGLPQLTSYDCEVNAPIQGSRNLLQGEELLRALDQVN

Ligands and cofactors

ID	Name	Formula	Copies
OGA	N-oxalylglycine	C4 H5 N O5	1
FE2	FE (II) ion	Fe	1

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

Primary citation

Structure of Factor-Inhibiting Hypoxia-Inducible Factor (Hif) Reveals Mechanism of Oxidative Modification of Hif-1Alpha. Elkins, J.M., Hewitson, K.S., McNeill, L.A. et al. J Biol Chem (2003) 278:1802-1806. DOI 10.1074/JBC.C200644200 · 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)
7A1K 1.99 Å, FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH ZN(II) AND…
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…

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