3ixs

X-ray diffraction
1.7Å resolution

Ring1B C-terminal domain/RYBP C-terminal domain Complex

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
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase RING2 Chains: A, C, E, G, I, K
Molecule details ›
Chains: A, C, E, G, I, K
Length: 111 amino acids
Theoretical weight: 12.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q99496 (Residues: 223-333; Coverage: 33%)
Gene names: BAP1, DING, HIPI3, RING1B, RNF2
Sequence domains: RAWUL domain RING finger- and WD40-associated ubiquitin-like
Structure domains: Ubiquitin-like (UB roll)
RING1 and YY1-binding protein Chains: B, D, F, H, J, L
Molecule details ›
Chains: B, D, F, H, J, L
Length: 37 amino acids
Theoretical weight: 4.11 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8N488 (Residues: 145-179; Coverage: 15%)
Gene names: DEDAF, RYBP, YEAF1
Sequence domains: Yaf2/RYBP C-terminal binding motif

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P1
Unit cell:
a: 37.894Å b: 56.549Å c: 100.352Å
α: 100.88° β: 90.61° γ: 100.49°
R-values:
R R work R free
0.204 0.203 0.234
Expression system: Escherichia coli BL21(DE3)