› 2c2l

X-ray diffraction
3.3Å resolution

Crystal structure of the CHIP U-box E3 ubiquitin ligase

Released:
DOI: 10.2210/pdb2c2l/pdb
PDB entry 2c2l coloured by chain, front view.
PDB entry 2c2l coloured by chain, side view.
PDB entry 2c2l coloured by chain, top view.
Source organisms:
Primary publication:
Chaperoned ubiquitylation--crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex.
Zhang M, Windheim M, Roe SM, Peggie M, Cohen P, Prodromou C, Pearl LH
Mol Cell 20 525-38 (2005)
PMID: 16307917

Function and Biology Details

Reactions 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
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139823 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase CHIP Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 281 amino acids
Theoretical weight: 32.73 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WUD1 (Residues: 24-304; Coverage: 92%)
Gene names: Chip, Stub1
Sequence domains:
Structure domains:
Heat shock protein HSP 90-alpha Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 9 amino acids
Theoretical weight: 1.08 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P07900 (Residues: 724-732; Coverage: 1%)
Gene names: HSP90A, HSP90AA1, HSPC1, HSPCA

Ligands and Environments

2 bound ligands:
Ligand SO4 7 x SO4
Ligand NI 4 x NI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: C2
Unit cell:
a: 76.042Å b: 204.406Å c: 144.709Å
α: 90° β: 90.75° γ: 90°
R-values:
R R work R free
0.248 0.248 0.286
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

66 review citations

RING domain E3 ubiquitin ligases.
Deshaies et al. (2009)
65 more

42 mentions without citation

Chaperoning Endoplasmic Reticulum-Associated Degradation (ERAD) and Protein Conformational Diseases.
Needham et al. (2019)
41 more