› 1pan

Solution NMR

A COMPARISON OF NMR SOLUTION STRUCTURES OF THE RECEPTOR BINDING DOMAINS OF PSEUDOMONAS AERUGINOSA PILI STRAINS PAO, KB7, AND PAK: IMPLICATIONS FOR RECEPTOR BINDING AND SYNTHETIC VACCINE DESIGN

Released:
DOI: 10.2210/pdb1pan/pdb
PDB entry 1pan coloured by chain, front view.
PDB entry 1pan coloured by chain, side view.
PDB entry 1pan coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
Comparison of NMR solution structures of the receptor binding domains of Pseudomonas aeruginosa pili strains PAO, KB7, and PAK: implications for receptor binding and synthetic vaccine design.
Campbell AP, McInnes C, Hodges RS, Sykes BD
Biochemistry 34 16255-68 (1995)
PMID: 8845350

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138162 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Type IV major pilin protein PilA Chain: A
Molecule details ›
Chain: A
Length: 18 amino acids
Theoretical weight: 1.87 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Not provided
UniProt:
  • Canonical: P04739 (Residues: 133-149; Coverage: 11%)
Gene names: PA4525, fimA, pilA

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Not provided

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Citations

3 review citations

Boehringer Mannheim award lecture 1995. La conference Boehringer Mannheim 1995. De novo design of alpha-helical proteins: basic research to medical applications.
Hodges RS. (1996)
2 more

5 mentions without citation

Arthropod 5-HT2 receptors: a neurohormonal receptor in decapod crustaceans that displays agonist independent activity resulting from an evolutionary alteration to the DRY motif.
Clark et al. (2004)
4 more