› 1a2p

X-ray diffraction
1.5Å resolution

BARNASE WILDTYPE STRUCTURE AT 1.5 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1a2p/pdb
PDB entry 1a2p coloured by chain, front view.
PDB entry 1a2p coloured by chain, side view.
PDB entry 1a2p coloured by chain, top view.
Source organism: Bacillus amyloliquefaciens
Primary publication:
Refinement and structural analysis of barnase at 1.5 A resolution.
Martin C, Richard V, Salem M, Hartley R, Mauguen Y
Acta Crystallogr D Biol Crystallogr 55 386-98 (1999)
PMID: 10089345

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132802 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonuclease Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 110 amino acids
Theoretical weight: 12.4 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00648 (Residues: 48-157; Coverage: 89%)
Sequence domains: ribonuclease
Structure domains: Microbial ribonucleases

Ligands and Environments

1 bound ligand:
Ligand ZN 3 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LURE BEAMLINE DW32
Spacegroup: P32
Unit cell:
a: 58.97Å b: 58.97Å c: 81.58Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.115 not available 0.174
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Barnase and binase: twins with distinct fates.
Ulyanova et al. (2011)
18 other articles

60 mentions without citation

Protonation and pK changes in protein-ligand binding.
Onufriev et al. (2013)
59 more