› 4auv

X-ray diffraction
2Å resolution

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo octamer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-190797 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Breast cancer metastasis-suppressor 1 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 35 amino acids
Theoretical weight: 4.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9HCU9 (Residues: 51-84; Coverage: 14%)
Gene name: BRMS1

Ligands and Environments

3 bound ligands:
Ligand CL 1 x CL
Ligand SO4 1 x SO4
Ligand ACY 1 x ACY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1, ESRF BEAMLINE ID23-1
Spacegroup: C2221
Unit cell:
a: 42.636Å b: 191.274Å c: 71.94Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.192 0.258
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 citation in other articles

Mcm10 self-association is mediated by an N-terminal coiled-coil domain.
Du et al. (2013)
2 more

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)