4KVM

The NatA (Naa10p/Naa15p) amino-terminal acetyltransferase complex bound to a bisubstrate analog

Summary for 4KVM

Related4KVO 4KVX
DescriptorN-terminal acetyltransferase A complex subunit nat1, N-terminal acetyltransferase A complex catalytic subunit ard1, bisubstrate analog inhibitor, ... (7 entities in total)
Functional Keywordsacetyltransferase, tpr repeats, amino-terminal acetylation, transferase-transferase inhibitor complex, transferase/transferase inhibitor
Biological sourceSchizosaccharomyces pombe (Fission yeast)
Cellular locationCytoplasm O74985 Q9UTI3
Total number of polymer chains12
Total molecular weight416919.98
Authors
Liszczak, G.P.,Marmorstein, R.Q. (deposition date: 2013-05-22, release date: 2013-07-31, Last modification date: 2013-10-23)
Primary citation
Liszczak, G.,Goldberg, J.M.,Foyn, H.,Petersson, E.J.,Arnesen, T.,Marmorstein, R.
Molecular basis for N-terminal acetylation by the heterodimeric NatA complex.
Nat.Struct.Mol.Biol., 20:1098-1105, 2013
PubMed: 23912279 (PDB entries with the same primary citation)
DOI: 10.1038/nsmb.2636
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.597 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.254101.6%8.5%7.2%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

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