› 4pbz

X-ray diffraction
2.15Å resolution

Structure of the human RbAp48-MTA1(670-695) complex

Released:
DOI: 10.2210/pdb4pbz/pdb
PDB entry 4pbz coloured by chain, front view.
PDB entry 4pbz coloured by chain, side view.
PDB entry 4pbz coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Insight into the architecture of the NuRD complex: structure of the RbAp48-MTA1 subcomplex.
Alqarni SS, Murthy A, Zhang W, Przewloka MR, Silva AP, Watson AA, Lejon S, Pei XY, Smits AH, Kloet SL, Wang H, Shepherd NE, Stokes PH, Blobel GA, Vermeulen M, Glover DM, Mackay JP, Laue ED
J Biol Chem 289 21844-55 (2014)
PMID: 24920672

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170742 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone-binding protein RBBP4 Chain: A
Molecule details ›
Chain: A
Length: 425 amino acids
Theoretical weight: 47.71 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q09028 (Residues: 1-425; Coverage: 100%)
Gene names: RBAP48, RBBP4
Sequence domains:
Structure domains: YVTN repeat-like/Quinoprotein amine dehydrogenase
Metastasis-associated protein MTA1 Chain: B
Molecule details ›
Chain: B
Length: 26 amino acids
Theoretical weight: 2.96 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q13330 (Residues: 670-695; Coverage: 4%)
Gene name: MTA1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P21
Unit cell:
a: 61.8Å b: 59.82Å c: 68.07Å
α: 90° β: 99.19° γ: 90°
R-values:
R R work R free
0.189 0.186 0.231
Expression systems:
  • Spodoptera frugiperda
  • Not provided

Quick links

Citations

13 review citations

Structure and function insights into the NuRD chromatin remodeling complex.
Torchy et al. (2015)
12 more

4 mentions without citation

The Methyl-CpG-Binding Domain 2 and 3 Proteins and Formation of the Nucleosome Remodeling and Deacetylase Complex.
Leighton et al. (2020)
3 more