› 2cbm

X-ray diffraction
2.03Å resolution

Crystal structure of the apo-form of a neocarzinostatin mutant evolved to bind testosterone.

Released:
DOI: 10.2210/pdb2cbm/pdb
PDB entry 2cbm coloured by chain, front view.
PDB entry 2cbm coloured by chain, side view.
PDB entry 2cbm coloured by chain, top view.
Source organism: Streptomyces carzinostaticus
Primary publication:
Structures of in vitro evolved binding sites on neocarzinostatin scaffold reveal unanticipated evolutionary pathways.
Drevelle A, Graille M, Heyd B, Sorel I, Ulryck N, Pecorari F, Desmadril M, van Tilbeurgh H, Minard P
J Mol Biol 358 455-71 (2006)
PMID: 16529771

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141217 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neocarzinostatin Chain: A
Molecule details ›
Chain: A
Length: 112 amino acids
Theoretical weight: 11.23 KDa
Source organism: Streptomyces carzinostaticus
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A3R9 (Residues: 35-146; Coverage: 99%)
Gene name: ncsA
Sequence domains: Neocarzinostatin family
Structure domains: Neocarzinostatin-like

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P6522
Unit cell:
a: 60.125Å b: 60.125Å c: 97.004Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.218 0.218 0.253
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Short peptides as biosensor transducers.
Pavan et al. (2012)
3 more

1 mention without citation

Controllable inhibition of cellular uptake of oxidized low-density lipoprotein: structure-function relationships for nanoscale amphiphilic polymers.
Iverson et al. (2010)