1p3l Summary

pdbe.org/1p3l
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Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants

The structure was published by Muthurajan, U.M., Bao, Y., Forsberg, L.J., et al., Dyer, P.N., White, C.L., and Luger, K., in 2004 in a paper entitled "Crystal structures of histone Sin mutant nucleosomes reveal altered protein-DNA interactions" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.4 Å and deposited in 2003.

The experimental data on which the structure is based was not deposited.

This entry contains 20 copies of 5 unique biopolymers (complete list).

The molecule most likely forms heterodecamers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Histone H3 P84233 (2-136) (H32_XENLA)search Xenopus laevissearch 99% 135 73%
E Histone H3 P84233 (2-136) (H32_XENLA)search Xenopus laevissearch 99% 135 73%
B Histone H4 P62799 (2-103) (H4_XENLA)search Xenopus laevissearch 99% 102 81%
F Histone H4 P62799 (2-103) (H4_XENLA)search Xenopus laevissearch 99% 102 81%
C Histone H2A P06897 (2-130) (H2A1_XENLA)search Xenopus laevissearch 92% 129 84%
G Histone H2A P06897 (2-130) (H2A1_XENLA)search Xenopus laevissearch 92% 129 84%
D Histone H2B P02281 (2-126) (H2B11_XENLA)search Xenopus laevissearch 97% 125 76%
H Histone H2B P02281 (2-126) (H2B11_XENLA)search Xenopus laevissearch 97% 125 76%


This entry contains 4 unique UniProt proteins:

UniProt accession Name Organism PDB
P84233 (2 - 136) Histone H3 Xenopus laevis
P62799 (2 - 103) Histone H4 Xenopus laevis
P06897 (2 - 130) Histone H2A Xenopus laevis
P02281 (2 - 126) Histone H2B Xenopus laevis

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, E (P84233) Nucleosome core histonessearch Histone, subunit Asearch PF00125: Core histone H2A/H2B/H3/H4search
B, F (P62799) Nucleosome core histonessearch Histone, subunit Asearch PF00125: Core histone H2A/H2B/H3/H4search
C, G (P06897) Nucleosome core histonessearch Histone, subunit Asearch PF00125: Core histone H2A/H2B/H3/H4search
D, H (P02281) Nucleosome core histonessearch Histone, subunit Asearch PF00125: Core histone H2A/H2B/H3/H4search

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A, E (P84233) protein heterodimerization activitysearch DNA bindingsearch protein bindingsearch nucleosomesearch chromosomesearch nucleoplasmsearch nucleussearch
B, F (P62799) DNA bindingsearch protein heterodimerization activitysearch protein bindingsearch nucleosomesearch nucleussearch chromosomesearch nucleosome assemblysearch
C, G (P06897) DNA bindingsearch protein heterodimerization activitysearch nucleussearch nucleosomesearch chromosomesearch
D, H (P02281) DNA bindingsearch protein heterodimerization activitysearch chromosomesearch nucleosomesearch nucleussearch

Chain InterPro annotation
A, E Histone H3/CENP-Asearch Histone coresearch Histone-foldsearch
B, F Histone H4search Histone coresearch Histone-foldsearch Histone H4, conserved sitesearch
C, G Histone H2Asearch Histone coresearch Histone-foldsearch
D, H Histone H2Bsearch Histone coresearch Histone-foldsearch