› 1pwb

X-ray diffraction
1.4Å resolution

High resolution crystal structure of an active recombinant fragment of human lung surfactant protein D with maltose

Released:
DOI: 10.2210/pdb1pwb/pdb
PDB entry 1pwb coloured by chain, front view.
PDB entry 1pwb coloured by chain, side view.
PDB entry 1pwb coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
High-resolution structural insights into ligand binding and immune cell recognition by human lung surfactant protein D.
Shrive AK, Tharia HA, Strong P, Kishore U, Burns I, Rizkallah PJ, Reid KB, Greenhough TJ
J Mol Biol 331 509-23 (2003)
PMID: 12888356

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152870 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Pulmonary surfactant-associated protein D Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 177 amino acids
Theoretical weight: 18.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P35247 (Residues: 199-375; Coverage: 50%)
Gene names: COLEC7, PSPD, SFTP4, SFTPD
Sequence domains:
Structure domains: Mannose-Binding Protein A, subunit A

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
2 bound ligands:
Ligand CA 9 x CA
Ligand GLC 2 x GLC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.1
Spacegroup: P21
Unit cell:
a: 55.48Å b: 108.3Å c: 55.78Å
α: 90° β: 91.43° γ: 90°
R-values:
R R work R free
0.205 0.205 0.228
Expression system: Escherichia coli

Quick links

Citations

15 review citations

The C-type lectin-like domain superfamily.
Zelensky et al. (2005)
14 more

8 mentions without citation

Playing hide and seek: how glycosylation of the influenza virus hemagglutinin can modulate the immune response to infection.
Tate et al. (2014)
7 more