› 1pnc

X-ray diffraction
1.6Å resolution

ACCURACY AND PRECISION IN PROTEIN CRYSTAL STRUCTURE ANALYSIS: TWO INDEPENDENT REFINEMENTS OF THE STRUCTURE OF POPLAR PLASTOCYANIN AT 173K

Released:
DOI: 10.2210/pdb1pnc/pdb
PDB entry 1pnc coloured by chain, front view.
PDB entry 1pnc coloured by chain, side view.
PDB entry 1pnc coloured by chain, top view.
Source organism: Populus nigra
Primary publication:
Accuracy and precision in protein crystal structure analysis: two independent refinements of the structure of poplar plastocyanin at 173 K.
Fields BA, Bartsch HH, Bartunik HD, Cordes F, Guss JM, Freeman HC
Acta Crystallogr D Biol Crystallogr 50 709-30 (1994)
PMID: 15299368

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-132379 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Plastocyanin A, chloroplastic Chain: A
Molecule details ›
Chain: A
Length: 99 amino acids
Theoretical weight: 10.49 KDa
Source organism: Populus nigra
Expression system: Not provided
UniProt:
  • Canonical: P00299 (Residues: 70-168; Coverage: 59%)
Gene name: PETE
Sequence domains: Copper binding proteins, plastocyanin/azurin family
Structure domains: Cupredoxins - blue copper proteins

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X31
Spacegroup: P212121
Unit cell:
a: 29.18Å b: 46.29Å c: 56.64Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.132 not available not available
Expression system: Not provided

Quick links

Citations

3 review citations

Structures of the high-valent metal-ion haem-oxygen intermediates in peroxidases, oxygenases and catalases.
Hersleth et al. (2006)
2 more

2 mentions without citation

Residue contacts predicted by evolutionary covariance extend the application of ab initio molecular replacement to larger and more challenging protein folds.
Simkovic et al. (2016)
1 more