9BF0: MID domain of human Argo2

MID domain of human Argo2 bound to UTP. Determined by X-ray diffraction at 1.78 Å resolution. Released 10 Jul 2024.

Method
X-ray diffraction
Resolution
1.78 Å
Organism
Homo sapiens
Chains
3
Atoms
3,529
Mol. weight
46.05 kDa
Ligands
UTP
Released
10 Jul 2024

Explore 9BF0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9BF0 contains 21 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
β-strand44811
β-strand451-45552
α-helix464-48017
β-strand48511
β-strand491-49442
α-helix498-5003
α-helix501-51111
β-strand517-52262
α-helix527-5337
α-helix534-5407
β-strand544-54852
α-helix549-5535
α-helix557-57115
Chain B: 7 helices, 6 β-strands
ElementResiduesLengthSheet
β-strand44813
β-strand451-45554
α-helix464-48017
β-strand48513
β-strand491-49444
α-helix498-5003
α-helix501-51111
β-strand517-52264
α-helix528-5336
α-helix534-5407
β-strand544-54854
α-helix550-5534
α-helix557-57115
Chain C: 7 helices, 6 β-strands
ElementResiduesLengthSheet
β-strand44815
β-strand451-45556
α-helix464-48017
β-strand48515
β-strand491-49446
α-helix498-5003
α-helix501-51111
β-strand517-52266
α-helix527-5337
α-helix534-5396
β-strand544-54856
α-helix550-5534
α-helix557-57115

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein argonaute-2A, B, Cprotein134Homo sapiensQ9UKV8 (AlphaFold model)
Sequence of entity 1 (A, B, C), FASTA
>9BF0_1 Protein argonaute-2 (chains A, B, C)
FHTGIEIKVWAIACFAPQRQCTEVHLKSFTEQLRKISRDAGMPIQGQPCFCKYAQGADSV
EPMFRHLKNTYAGLQLVVVILPGKTPVYAEVKRVGDTVLGMATQCVQMKNVQRTTPQTLS
NLCLKINVKLGGVN

Ligands and cofactors

IDNameFormulaCopies
UTPUridine 5'-triphosphateC9 H15 N2 O15 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:

Browse structure collections

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