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

Extended structure of citidine deaminase domain of APOBEC3G. Determined by solution NMR. Released 2 Jun 2009.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
1,605
Mol. weight
23.58 kDa
Ligands
ZN
Released
2 Jun 2009

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

Secondary structure: helices and β-sheets

2KEM contains 8 α-helices and 11 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, 11 β-strands

ElementResiduesLengthSheet
α-helix12-165
β-strand3111
β-strand34-3742
α-helix68-7912
β-strand8113
β-strand8513
β-strand86-8942
β-strand92-9321
α-helix99-1057
α-helix106-1105
β-strand116-11722
β-strand11814
β-strand120-12121
α-helix132-1376
α-helix138-1425
β-strand14414
β-strand14711
α-helix150-16011
α-helix173-18917

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
DNA dC->dU-editing enzyme APOBEC-3GAprotein202Homo sapiensQ9HC16 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2KEM_1 DNA dC->dU-editing enzyme APOBEC-3G (chains A)
GPLGSPGFEILRHSMDPPTFTFNFNNEPWVRGRHETYLCYEVERMHNDTWVKLNQRRGFL
ANQAPHKHGFLEGRHAELCFLDVIPFWKLDLDQDYRVTCFTSWSPCFSCAQEMAKFISKN
KHVSLCIKTARIYDDQGRAQEGLRTLAEAGAKISIMTYSEFKHCWDTFVDHQGAPFQPWD
GLDEHSQDLSGRLRAILQNQEN

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn1

Primary citation

An extended structure of the APOBEC3G catalytic domain suggests a unique holoenzyme model. Harjes, E., Gross, P.J., Chen, K.M. et al. J Mol Biol (2009) 389:819-832. DOI 10.1016/j.jmb.2009.04.031 · PubMed

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

Browse structure collections

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