› 5z6d

X-ray diffraction
1.6Å resolution

Crystal structure of Abundant Perithecial Protein (APP) from Neurospora crassa

Released:
DOI: 10.2210/pdb5z6d/pdb
Model geometry
Fit model/data
PDB entry 5z6d coloured by chain, front view.
PDB entry 5z6d coloured by chain, side view.
PDB entry 5z6d coloured by chain, top view.
Source organism: Neurospora crassa OR74A
Primary publication:
Interface interactions between βγ-crystallin domain and Ig-like domain render Ca2+ -binding site inoperative in abundant perithecial protein of Neurospora crassa.
Swaroop Srivastava S, Raman R, Kiran U, Garg R, Chadalawada S, Pawar AD, Sankaranarayanan R, Sharma Y
Mol Microbiol 110 955-972 (2018)
PMID: 30216631

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181913 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DUF1881 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 215 amino acids
Theoretical weight: 23.88 KDa
Source organism: Neurospora crassa OR74A
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q7RY31 (Residues: 1-207; Coverage: 100%)
Gene names: NCU04533, app
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: P21
Unit cell:
a: 46.319Å b: 40.168Å c: 103.542Å
α: 90° β: 96.81° γ: 90°
R-values:
R R work R free
0.186 0.184 0.229
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Chemical Properties Determine Solubility and Stability in βγ-Crystallins of the Eye Lens.
Rocha et al. (2021)
1 other article