5hkx

X-ray diffraction
1.85Å resolution

Crystal Structure of c-Cbl TKBD-RING domains (Y371E mutant) Refined to 1.85 A Resolution

Released:
Source organism: Homo sapiens
Entry authors: Lovell S, Battaile KP, Mehzabeen N, Zhang N, Cooper A, Gao P, Perez RP

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:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-149756 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase CBL Chain: A
Molecule details ›
Chain: A
Length: 392 amino acids
Theoretical weight: 45.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P22681 (Residues: 47-435; Coverage: 43%)
Gene names: CBL, CBL2, RNF55
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P21
Unit cell:
a: 44.075Å b: 108.737Å c: 49.304Å
α: 90° β: 115.31° γ: 90°
R-values:
R R work R free
0.169 0.167 0.214
Expression system: Escherichia coli BL21(DE3)