› 4hy4

X-ray diffraction
1.25Å resolution

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
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171717 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Baculoviral IAP repeat-containing protein 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 115 amino acids
Theoretical weight: 13.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q13490 (Residues: 260-352; Coverage: 15%)
Gene names: API1, BIRC2, MIHB, RNF48
Sequence domains: Inhibitor of Apoptosis domain
Structure domains: Inhibitor Of Apoptosis Protein (2mihbC-IAP-1); Chain A

Ligands and Environments

2 bound ligands:
Ligand ZN 2 x ZN
Ligand 1BG 2 x 1BG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: P212121
Unit cell:
a: 30.645Å b: 68.591Å c: 117.592Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.153 0.152 0.17
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Synthesis of complex unnatural fluorine-containing amino acids.
Brittain et al. (2020)
14 other articles

1 mention without citation

The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins.
Chakraborty et al. (2013)