7D7U: Ago2 MID domain

Crystal structure of Ago2 MID domain in complex with 8-Br-adenosin-5'-monophosphate. Determined by X-ray diffraction at 2.0 Å resolution. Released 25 Nov 2020.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Homo sapiens
Chains
3
Atoms
3,401
Mol. weight
47.67 kDa
Ligands
8BR
Released
25 Nov 2020

Explore 7D7U in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7D7U contains 23 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.

Chain A: 7 helices, 6 β-strands

ElementResiduesLengthSheet
α-helix441-4433
β-strand44811
β-strand451-45552
α-helix464-48017
β-strand48511
β-strand491-49442
α-helix498-5003
α-helix501-51111
β-strand517-52262
α-helix528-53811
β-strand544-54852
α-helix550-5534
α-helix557-57115
Chain B: 8 helices, 6 β-strands
ElementResiduesLengthSheet
α-helix441-4433
β-strand44813
β-strand451-45554
α-helix464-48017
β-strand48513
β-strand492-49434
α-helix498-5003
α-helix501-51111
β-strand517-52264
α-helix528-5336
α-helix534-5407
β-strand544-54854
α-helix549-5535
α-helix557-57115
Chain C: 8 helices, 6 β-strands
ElementResiduesLengthSheet
β-strand44815
β-strand451-45556
α-helix464-48017
α-helix4841
β-strand48515
α-helix4861
β-strand491-49446
α-helix498-5003
α-helix501-51111
β-strand517-52266
α-helix528-53710
β-strand544-54856
α-helix549-5535
α-helix557-57115

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein argonaute-2A, B, Cprotein139Homo sapiensQ9UKV8 (AlphaFold model)
Sequence of entity 1 (A, B, C), FASTA
>7D7U_1 Protein argonaute-2 (chains A, B, C)
KQFHTGIEIKVWAIACFAPQRQCTEVHLKSFTEQLRKISRDAGMPIQGQPCFCKYAQGAD
SVEPMFRHLKNTYAGLQLVVVILPGKTPVYAEVKRVGDTVLGMATQCVQMKNVQRTTPQT
LSNLCLKINVKLGGVNNIL

Ligands and cofactors

IDNameFormulaCopies
8BR8-bromo-adenosine-5'-monophosphateC10 H13 Br N5 O7 P3

Primary citation

siRNA potency enhancement via chemical modifications of nucleotide bases at the 5'-end of the siRNA guide strand. Shinohara, F., Oashi, T., Harumoto, T. et al. RNA (2021) 27:163-173. DOI 10.1261/rna.073783.119 · 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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