› 4npn

X-ray diffraction
1.63Å resolution

Crystal structure of human tetra-SUMO-2

Released:
DOI: 10.2210/pdb4npn/pdb
PDB entry 4npn coloured by chain, front view.
PDB entry 4npn coloured by chain, side view.
PDB entry 4npn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural analysis of poly-SUMO chain recognition by the RNF4-SIMs domain.
Kung CC, Naik MT, Wang SH, Shih HM, Chang CC, Lin LY, Chen CL, Ma C, Chang CF, Huang TH
Biochem J 462 53-65 (2014)
PMID: 24844634

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo tetramer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158455 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Small ubiquitin-related modifier 2 Chain: A
Molecule details ›
Chain: A
Length: 102 amino acids
Theoretical weight: 11.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P61956 (Residues: 12-93; Coverage: 86%)
Gene names: SMT3B, SMT3H2, SUMO2
Sequence domains: Ubiquitin-2 like Rad60 SUMO-like
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: R3
Unit cell:
a: 75.123Å b: 75.123Å c: 33.116Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.199 0.198 0.218
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Ubiquitin-like Protein Conjugation: Structures, Chemistry, and Mechanism.
Cappadocia et al. (2018)
1 more

1 mention without citation

An "up" oriented methionine-aromatic structural motif in SUMO is critical for its stability and activity.
Chatterjee et al. (2021)