2ILM: Factor Inhibiting HIF-1 Alpha D201A Mutant

Factor Inhibiting HIF-1 Alpha D201A Mutant in Complex with FE(II), Alpha-Ketoglutarate and HIF-1 Alpha 35mer. Determined by X-ray diffraction at 2.3 Å resolution. Released 14 Aug 2007.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,910
Mol. weight: 45.52 kDa
Ligands: AKG, BCT, FE2
Released: 14 Aug 2007

Explore 2ILM in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2ILM contains 22 α-helices and 19 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: 22 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	16-17	2
β-strand	18	1	1
α-helix	19	1
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	78-81	4
β-strand	92-95	4	3
β-strand	99	1	2
α-helix	105-107	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	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	300-303	4
α-helix	310-311	2
α-helix	312-329	18
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)
Hypoxia-inducible factor 1 alpha	S	protein	41		Q16665 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2ILM_1 Hypoxia-inducible factor 1 alpha inhibitor (chains A)
MAATAAEAVASGSGEPREEAGALGPAWDESQLRSYSFPTRPIPRLSQSDPRAEELIENEE
PVVLTDTNLVYPALKWDLEYLQENIGNGDFSVYSASTHKFLYYDEKKMANFQNFKPRSNR
EEMKFHEFVEKLQDIQQRGGEERLYLQQTLNDTVGRKIVMDFLGFNWNWINKQQGKRGWG
QLTSNLLLIGMEGNVTPAHYAEQQNFFAQIKGYKRCILFPPDQFECLYPYPVHHPCDRQS
QVDFDNPDYERFPNFQNVVGYETVVGPGDVLYIPMYWWHHIESLLNGGITITVNFWYKGA
PTPKRIEYPLKAHQKVAIMRNIEKMLGEALGNPQEVGPLLNTMIKGRYN

Sequence of entity 2 (S), FASTA

>2ILM_2 Hypoxia-inducible factor 1 alpha (chains S)
SMDESGLPQLTSYDCEVNAPIQGSRNLLQGEELLRALDQVN

Ligands and cofactors

ID	Name	Formula	Copies
AKG	2-oxoglutaric acid	C5 H6 O5	1
BCT	Bicarbonate ion	C H O3	1
FE2	FE (II) ion	Fe	1

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

Primary citation

Evidence that two enzyme-derived histidine ligands are sufficient for iron binding and catalysis by factor inhibiting HIF (FIH). Hewitson, K.S., Holmes, S.L., Ehrismann, D. et al. J Biol Chem (2008) 283:25971-25978. DOI 10.1074/jbc.M804999200 · 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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