4kbq

X-ray diffraction
2.91Å resolution

Structure of the CHIP-TPR domain in complex with the Hsc70 Lid-Tail domains

Released:

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:
Non-polymer only dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase CHIP Chains: A, B
Molecule details ›
Chains: A, B
Length: 139 amino acids
Theoretical weight: 15.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9UNE7 (Residues: 21-154; Coverage: 44%)
Gene names: CHIP, PP1131, STUB1
Sequence domains: Anaphase-promoting complex, cyclosome, subunit 3
Structure domains: Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Heat shock cognate 71 kDa protein Chains: C, D
Molecule details ›
Chains: C, D
Length: 101 amino acids
Theoretical weight: 11.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P11142 (Residues: 541-646; Coverage: 14%)
Gene names: HSC70, HSP73, HSPA10, HSPA8

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P6122
Unit cell:
a: 78.5Å b: 78.5Å c: 424.7Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.227 0.224 0.263
Expression system: Escherichia coli BL21(DE3)