› 2rno

Solution NMR

Solution Structure of the N-terminal SAP Domain of SUMO E3 Ligases from Oryza sativa

Released:
DOI: 10.2210/pdb2rno/pdb
PDB entry 2rno coloured by chain, ensemble of 20 models, front view.
PDB entry 2rno coloured by chain, ensemble of 20 models, side view.
PDB entry 2rno coloured by chain, ensemble of 20 models, top view.
Source organism: Oryza sativa Japonica Group
Primary publication:
Solution structures and DNA binding properties of the N-terminal SAP domains of SUMO E3 ligases from Saccharomyces cerevisiae and Oryza sativa.
Suzuki R, Shindo H, Tase A, Kikuchi Y, Shimizu M, Yamazaki T
Proteins 75 336-47 (2009)
PMID: 18831036

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179842 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 SUMO-protein ligase SIZ1 Chain: A
Molecule details ›
Chain: A
Length: 110 amino acids
Theoretical weight: 12.39 KDa
Source organism: Oryza sativa Japonica Group
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6L4L4 (Residues: 2-105; Coverage: 12%)
Gene names: LOC_Os05g03430, OSJNBb0079L11.3, Os05g0125000, SIZ1
Sequence domains: SAP domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 89%
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Evolvement of LEM proteins as chromatin tethers at the nuclear periphery.
Brachner et al. (2011)
8 more

1 mention without citation

Plant SUMO E3 Ligases: Function, Structural Organization, and Connection With DNA.
Jmii et al. (2021)