4Z1V: Factor Inhibiting HIF

Structure of Factor Inhibiting HIF (FIH) in complex with Fe, NO, and NOG. Determined by X-ray diffraction at 2.1 Å resolution. Released 13 Jan 2016.

Method
X-ray diffraction
Resolution
2.1 Å
Organism
Homo sapiens
Chains
1
Atoms
2,904
Mol. weight
41.43 kDa
Ligands
NO, FE, OGA
Released
13 Jan 2016

Explore 4Z1V in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4Z1V contains 21 α-helices and 21 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: 21 helices, 21 β-strands

ElementResiduesLengthSheet
α-helix16-172
β-strand18-1921
α-helix20-223
β-strand24-2521
α-helix29-313
β-strand39-4132
α-helix42-432
β-strand44-4523
α-helix50-578
β-strand62-6433
α-helix71-755
α-helix78-847
β-strand89-9573
β-strand9912
α-helix105-1084
β-strand120-12453
α-helix125-13612
β-strand143-14973
α-helix156-1638
α-helix167-17610
β-strand182-18433
β-strand186-19053
β-strand195-19952
β-strand204-21183
β-strand214-21962
α-helix221-2233
α-helix224-2274
β-strand22914
α-helix230-2312
β-strand23912
β-strand24014
α-helix253-2575
β-strand260-26562
β-strand270-27343
β-strand278-28362
α-helix2841
β-strand290-29783
α-helix298-3036
α-helix310-3112
α-helix312-32918
α-helix333-3353
α-helix336-3449

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Hypoxia-inducible factor 1-alpha inhibitorAprotein352Homo sapiensQ9NWT6 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4Z1V_1 Hypoxia-inducible factor 1-alpha inhibitor (chains A)
GSHMAATAAEAVASGSGEPREEAGALGPAWDESQLRSYSFPTRPIPRLSQSDPRAEELIE
NEEPVVLTDTNLVYPALKWDLEYLQENIGNGDFSVYSASTHKFLYYDEKKMANFQNFKPR
SNREEMKFHEFVEKLQDIQQRGGEERLYLQQTLNDTVGRKIVMDFLGFNWNWINKQQGKR
GWGQLTSNLLLIGMEGNVTPAHYDEQQNFFAQIKGYKRCILFPPDQFECLYPYPVHHPCD
RQSQVDFDNPDYERFPNFQNVVGYETVVGPGDVLYIPMYWWHHIESLLNGGITITVNFWY
KGAPTPKRIEYPLKAHQKVAIMRNIEKMLGEALGNPQEVGPLLNTMIKGRYN

Ligands and cofactors

IDNameFormulaCopies
NONitric oxideN O1
FEFE (III) ionFe1
OGAN-oxalylglycineC4 H5 N O51

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

Primary citation

Substrate Promotes Productive Gas Binding in the alpha-Ketoglutarate-Dependent Oxygenase FIH. Taabazuing, C.Y., Fermann, J., Garman, S. et al. Biochemistry (2016) 55:277-286. DOI 10.1021/acs.biochem.5b01003 · PubMed

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

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