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2YBG

Structure of Lys120-acetylated p53 core domain

Summary for 2YBG
Entry DOI10.2210/pdb2ybg/pdb
Related1A1U 1AIE 1C26 1DT7 1GZH 1H26 1HS5 1JSP 1KZY 1MA3 1OLG 1OLH 1PES 1PET 1SAE 1SAF 1SAH 1SAJ 1SAK 1SAL 1TSR 1TUP 1UOL 1XQH 1YCQ 1YCR 1YCS 2AC0 2ADY 2AHI 2ATA 2B3G 2BIM 2BIN 2BIO 2BIP 2BIQ 2FEJ 2FOJ 2FOO 2GS0 2H1L 2J0Z 2J10 2J11 2J1W 2J1X 2J1Y 2J1Z 2J20 2J21 2VUK 2WGX 2X0U 2X0V 2X0W 2XWR 3SAK
DescriptorCELLULAR TUMOR ANTIGEN P53, ZINC ION (3 entities in total)
Functional Keywordscell cycle, tumor suppressor, cancer, lysine acetylation, apoptosis
Biological sourceHOMO SAPIENS (HUMAN)
Cellular locationCytoplasm. Isoform 1: Nucleus. Isoform 2: Nucleus. Isoform 3: Nucleus. Isoform 4: Nucleus. Isoform 7: Nucleus. Isoform 8: Nucleus. Isoform 9: Cytoplasm: P04637
Total number of polymer chains4
Total formula weight90448.08
Authors
Arbely, E.,Allen, M.D.,Joerger, A.C.,Fersht, A.R. (deposition date: 2011-03-08, release date: 2011-05-04, Last modification date: 2011-07-13)
Primary citationArbely, E.,Natan, E.,Brandt, T.,Allen, M.D.,Veprintsev, D.B.,Robinson, C.V.,Chin, J.W.,Joerger, A.C.,Fersht, A.R.
Acetylation of Lysine 120 of P53 Endows DNA- Binding Specificity at Effective Physiological Salt Concentration.
Proc.Natl.Acad.Sci.USA, 108:8251-, 2011
Cited by
PubMed: 21525412
DOI: 10.1073/PNAS.1105028108
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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