2KBO: DNA dC->dU-editing enzyme APOBEC-3G

Structure, interaction, and real-time monitoring of the enzymatic reaction of wild type APOBEC3G. Determined by solution NMR. Released 3 Feb 2009.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
1,611
Mol. weight
22.99 kDa
Ligands
ZN
Released
3 Feb 2009

Explore 2KBO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2KBO contains 8 α-helices and 5 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: 8 helices, 5 β-strands

ElementResiduesLengthSheet
α-helix9-146
β-strand31-3881
β-strand41-4221
α-helix68-7912
β-strand86-9271
α-helix99-1068
α-helix107-1115
β-strand115-12171
α-helix130-1323
α-helix133-1419
β-strand143-14751
α-helix150-16011
α-helix174-18916

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
DNA dC->dU-editing enzyme APOBEC-3GAprotein194Homo sapiensQ9HC16 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2KBO_1 DNA dC->dU-editing enzyme APOBEC-3G (chains A)
HMLRHSMDPPTFTFNFNNEPWVRGRHETYLCYEVERMHNDTWVLLNQRRGFLCNQAPHKH
GFLEGRHAELCFLDVIPFWKLDLDQDYRVTCFTSWSPCFSCAQEMAKFISKNKHVSLCIF
TARIYDDQGRCQEGLRTLAEAGAKISIMTYSEFKHCWDTFVDHQGCPFQPWDGLDEHSQD
LSGRLRAILQNQEN

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn1

Primary citation

Structure, interaction and real-time monitoring of the enzymatic reaction of wild-type APOBEC3G. Furukawa, A., Nagata, T., Matsugami, A. et al. EMBO J (2009) 28:440-451. DOI 10.1038/emboj.2008.290 · PubMed

Other PDB entries of the same protein (UniProt Q9HC16 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 2KBO directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.