› 2xre

X-ray diffraction
2.45Å resolution

Detection of cobalt in previously unassigned human SENP1 structure

Released:
DOI: 10.2210/pdb2xre/pdb
PDB entry 2xre coloured by chain, front view.
PDB entry 2xre coloured by chain, side view.
PDB entry 2xre coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The role of Co²+ in the crystallization of human SENP1 and comments on the limitations of automated refinement protocols.
Rimsa V, Eadsforth T, Hunter WN
Acta Crystallogr Sect F Struct Biol Cryst Commun 67 442-5 (2011)
PMID: 21505236

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192807 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sentrin-specific protease 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 230 amino acids
Theoretical weight: 27.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9P0U3 (Residues: 415-644; Coverage: 36%)
Gene name: SENP1
Sequence domains: Ulp1 protease family, C-terminal catalytic domain
Structure domains: Adenoviral Proteinase; Chain A

Ligands and Environments

2 bound ligands:
Ligand GOL 10 x GOL
Ligand CO 1 x CO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P3121
Unit cell:
a: 71.981Å b: 71.981Å c: 200.64Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.241 0.237 0.317
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 citations in other articles

Structures of Pseudomonas aeruginosa β-ketoacyl-(acyl-carrier-protein) synthase II (FabF) and a C164Q mutant provide templates for antibacterial drug discovery and identify a buried potassium ion and a ligand-binding site that is an artefact of the crystal form.
Baum et al. (2015)

2 mentions without citation

Advances in the development of SUMO specific protease (SENP) inhibitors.
Kumar et al. (2015)
1 more