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:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145679 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase CHIP
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:
Sequence domains: Anaphase-promoting complex, cyclosome, subunit 3
Structure domains: Tetratricopeptide repeat domain
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%)
Sequence domains: Anaphase-promoting complex, cyclosome, subunit 3
Structure domains: Tetratricopeptide repeat domain
Heat shock cognate 71 kDa protein
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:
Structure domains: Substrate Binding Domain Of Dnak; Chain:A; Domain 2
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%)
Structure domains: Substrate Binding Domain Of Dnak; Chain:A; Domain 2
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ALS BEAMLINE 4.2.2
Spacegroup:
P6122
Expression system: Escherichia coli BL21(DE3)
