3gbw

X-ray diffraction
1.32Å resolution

Crystal structure of the first PHR domain of the Mouse Myc-binding protein 2 (MYCBP-2)

Released:

Function and Biology Details

Reaction catalysed:
(1a) [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [RCR-type E3 ubiquitin transferase]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [RCR-type E3 ubiquitin transferase]-S-ubiquitinyl-L-cysteine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-182021 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase MYCBP2 Chain: A
Molecule details ›
Chain: A
Length: 164 amino acids
Theoretical weight: 17.82 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7TPH6 (Residues: 1229-1390; Coverage: 3%)
Gene names: Mycbp2, Pam, Phr1
Sequence domains: PHR domain
Structure domains: PHR domain

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: P212121
Unit cell:
a: 41.688Å b: 57.767Å c: 64.633Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.164 0.162 0.189
Expression system: Escherichia coli