X-ray diffraction
1.72Å resolution

Crystal structure of the human retinoblastoma-binding protein 9 (RBBP-9). NESG target HR2978


Function and Biology Details

Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Serine hydrolase RBBP9 Chains: A, B
Molecule details ›
Chains: A, B
Length: 194 amino acids
Theoretical weight: 22.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: O75884 (Residues: 1-186; Coverage: 100%)
Gene names: BOG, RBBP10, RBBP9
Sequence domains: Serine hydrolase
Structure domains: alpha/beta hydrolase

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P21
Unit cell:
a: 37.081Å b: 130.34Å c: 39.047Å
α: 90° β: 115.87° γ: 90°
R R work R free
0.183 0.183 0.203
Expression system: Escherichia coli