2faz

X-ray diffraction
2Å resolution

Ubiquitin-Like Domain of Human Nuclear Zinc Finger Protein NP95

Released:
Source organism: Homo sapiens
Entry authors: Walker JR, Wybenga-Groot L, Doherty RS, Finerty Jr PJ, Newman E, Mackenzie FM, Weigelt J, Sundstrom M, Arrowsmith C, Edwards A, Bochkarev A, Dhe-Paganon S, Structural Genomics Consortium (SGC)

Function and Biology Details

Reaction catalysed:
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-188767 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase UHRF1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 78 amino acids
Theoretical weight: 9.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q96T88 (Residues: 1-76; Coverage: 10%)
Gene names: ICBP90, NP95, RNF106, UHRF1
Sequence domains: Ubiquitin family
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: APS BEAMLINE 19-BM
Spacegroup: P6522
Unit cell:
a: 89.554Å b: 89.554Å c: 108.279Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.22 0.218 0.252
Expression system: Escherichia coli BL21