9BEZ: MID domain of human Argo2

MID domain of human Argo2 bound to RNA. Determined by X-ray diffraction at 1.9 Å resolution. Released 10 Jul 2024.

Method
X-ray diffraction
Resolution
1.9 Å
Organism
Homo sapiens
Chains
3
Atoms
3,265
Mol. weight
46.78 kDa
Ligands
A1ANT
Released
10 Jul 2024

Explore 9BEZ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9BEZ contains 24 α-helices and 18 β-strands across 3 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.

Chains A and B: 8 helices, 6 β-strands

ElementResiduesLengthSheet
α-helix442-4432
β-strand44811
β-strand451-45552
α-helix464-48017
β-strand48511
β-strand491-49442
α-helix498-5003
α-helix501-51111
β-strand517-52262
α-helix527-5348
α-helix535-5406
β-strand544-54852
α-helix550-5534
α-helix557-57115
Chain C: 8 helices, 6 β-strands
ElementResiduesLengthSheet
α-helix441-4433
β-strand44815
β-strand451-45556
α-helix464-48017
β-strand48515
β-strand491-49446
α-helix498-5003
α-helix501-51111
β-strand517-52266
α-helix527-5348
α-helix535-5406
β-strand543-54866
α-helix550-5534
α-helix557-57014

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein argonaute-2A, B, Cprotein136Homo sapiensQ9UKV8 (AlphaFold model)
Sequence of entity 1 (A, B, C), FASTA
>9BEZ_1 Protein argonaute-2 (chains A, B, C)
KQFHTGIEIKVWAIACFAPQRQCTEVHLKSFTEQLRKISRDAGMPIQGQPCFCKYAQGAD
SVEPMFRHLKNTYAGLQLVVVILPGKTPVYAEVKRVGDTVLGMATQCVQMKNVQRTTPQT
LSNLCLKINVKLGGVN

Ligands and cofactors

IDNameFormulaCopies
A1ANT[(3~{S},4~{R},5~{R})-5-[5-methyl-2,4-bis(oxidanylidene)pyrimidin-1-yl]-4-oxidan…C9 H15 N2 O14 P33

Primary citation

Structure and Stability of Ago2 MID-Nucleotide Complexes: All-in-One (Drop) His 6 -SUMO Tag Removal, Nucleotide Binding, and Crystal Growth. Lei, L., Harp, J.M., Chaput, J.C. et al. Curr Protoc (2024) 4:e1088-e1088. DOI 10.1002/cpz1.1088 · PubMed

Other PDB entries of the same protein (UniProt Q9UKV8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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