2xph

X-ray diffraction
2.4Å resolution

Crystal structure of human SENP1 with the bound cobalt

Released:
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.
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

Structure analysis Details

Assembly composition:
monomeric (preferred)
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: 238 amino acids
Theoretical weight: 28.08 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:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P3121
Unit cell:
a: 71.172Å b: 71.172Å c: 199.988Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.231 0.227 0.313
Expression system: Escherichia coli BL21(DE3)