5ZBZ: DEAD domain of Human eIF4A with sanguinarine

Crystal structure of the DEAD domain of Human eIF4A with sanguinarine. Determined by X-ray diffraction at 1.31 Å resolution. Released 20 Feb 2019.

Method
X-ray diffraction
Resolution
1.31 Å
Organism
Homo sapiens
Chains
1
Atoms
1,896
Mol. weight
25.36 kDa
Ligands
MLI, SAU
Released
20 Feb 2019

Explore 5ZBZ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5ZBZ contains 11 α-helices and 7 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: 11 helices, 7 β-strands

ElementResiduesLengthSheet
α-helix34-363
α-helix41-5010
α-helix57-6711
β-strand72-7541
α-helix82-9312
β-strand103-10641
α-helix110-12314
β-strand131-13441
α-helix137-1393
α-helix140-14910
β-strand154-15741
α-helix159-1679
β-strand178-18251
α-helix184-1896
α-helix193-20210
β-strand208-21361
α-helix218-22710
β-strand232-23541

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Eukaryotic initiation factor 4A-IAprotein220Homo sapiensP60842 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5ZBZ_1 Eukaryotic initiation factor 4A-I (chains A)
GEGVIESNWNEIVDSFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQS
GTGKTATFAISILQQIELDLKATQALVLAPTRELAQQIQKVVMALGDYMGASCHACIGGT
NVRAEVQKLQMEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQIYD
IFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRILVKK

Ligands and cofactors

IDNameFormulaCopies
MLIMalonate ionC3 H2 O41
SAU13-methyl[1,3]benzodioxolo[5,6-c][1,3]dioxolo[4,5-i]phenanthridin-13-iumC20 H14 N O41

Primary citation

Targeting the N Terminus of eIF4AI for Inhibition of Its Catalytic Recycling. Jiang, C., Tang, Y., Ding, L. et al. Cell Chem Biol (2019) 26:1417-1426.e5. DOI 10.1016/j.chembiol.2019.07.010 · PubMed

Other PDB entries of the same protein (UniProt P60842 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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