› 3bd0

X-ray diffraction
3.01Å resolution

Crystal structure of Memo, form II

Released:
DOI: 10.2210/pdb3bd0/pdb
PDB entry 3bd0 coloured by chain, front view.
PDB entry 3bd0 coloured by chain, side view.
PDB entry 3bd0 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Memo is homologous to nonheme iron dioxygenases and binds an ErbB2-derived phosphopeptide in its vestigial active site.
Qiu C, Lienhard S, Hynes NE, Badache A, Leahy DJ
J Biol Chem 283 2734-40 (2008)
PMID: 18045866

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195177 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein MEMO1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 293 amino acids
Theoretical weight: 33.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y316 (Residues: 5-297; Coverage: 99%)
Gene names: C2orf4, CGI-27, MEMO, MEMO1, NS5ATP7
Sequence domains: Memo-like protein
Structure domains: LigB-like

Ligands and Environments

1 bound ligand:
Ligand PEG 1 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: P21212
Unit cell:
a: 139.877Å b: 88.307Å c: 97.051Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.213 0.28
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Finding MEMO-Emerging Evidence for MEMO1's Function in Development and Disease.
Schotanus et al. (2020)
1 more

1 mention without citation

Oxidative opening of the aromatic ring: Tracing the natural history of a large superfamily of dioxygenase domains and their relatives.
Burroughs et al. (2019)