› 5hh7

X-ray diffraction
1.9Å resolution

crystal structure of Arabidopsis ORC1b BAH-PHD cassette in complex with unmodified H3 peptide

Released:
DOI: 10.2210/pdb5hh7/pdb
PDB entry 5hh7 coloured by chain, front view.
PDB entry 5hh7 coloured by chain, side view.
PDB entry 5hh7 coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Structural Basis for the Unique Multivalent Readout of Unmodified H3 Tail by Arabidopsis ORC1b BAH-PHD Cassette.
Li S, Yang Z, Du X, Liu R, Wilkinson AW, Gozani O, Jacobsen SE, Patel DJ, Du J
Structure 24 486-94 (2016)
PMID: 26876097

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157789 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Origin of replication complex subunit 1B Chain: A
Molecule details ›
Chain: A
Length: 233 amino acids
Theoretical weight: 27.4 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9SU24 (Residues: 118-349; Coverage: 29%)
Gene names: At4g12620, ORC1B, T1P17.210, UNE13
Sequence domains:
Histone H3.1 Chain: P
Molecule details ›
Chain: P
Length: 15 amino acids
Theoretical weight: 1.57 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: P59226 (Residues: 2-16; Coverage: 11%)
Gene names: At1g09200, At3g27360, At5g10390, At5g10400, At5g65360, F12B17_250, F12B17_260, HTR1, HTR13, HTR2, HTR3, HTR9, K1G2.8, MNA5.9, T12M4.9

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P43
Unit cell:
a: 64.408Å b: 64.408Å c: 79.633Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.194 0.205
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Structure and mechanism of plant histone mark readers.
Liu et al. (2018)
2 more

2 mentions without citation

Insights into newly discovered marks and readers of epigenetic information.
Andrews et al. (2016)
1 more