› 5osq

X-ray diffraction
2.05Å resolution

ZP-N domain of mammalian sperm receptor ZP3 (crystal form II, processed in P21221)

Released:
DOI: 10.2210/pdb5osq/pdb
PDB entry 5osq coloured by chain, front view.
PDB entry 5osq coloured by chain, side view.
PDB entry 5osq coloured by chain, top view.
Source organisms:
Primary publication:
Crystal structure of the ZP-N domain of ZP3 reveals the core fold of animal egg coats.
Monné M, Han L, Schwend T, Burendahl S, Jovine L
Nature 456 653-7 (2008)
PMID: 19052627

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-142514 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Maltose/maltodextrin-binding periplasmic protein; Processed zona pellucida sperm-binding protein 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 481 amino acids
Theoretical weight: 52.95 KDa
Source organisms: Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0AEX9 (Residues: 27-393; Coverage: 99%)
  • Canonical: P10761 (Residues: 42-143; Coverage: 25%)
Gene names: JW3994, Zp-3, Zp3, Zpc, b4034, malE
Sequence domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
2 bound ligands:
Ligand CA 6 x CA
Ligand PGE 1 x PGE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Unit cell:
a: 91.34Å b: 92.16Å c: 140.95Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.209 0.241
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

27 review citations

Disulfide bonding in protein biophysics.
Fass D. (2012)
26 more

1 mention without citation

Molecular basis of egg coat cross-linking sheds light on ZP1-associated female infertility.
Nishimura et al. (2019)