› 1g6e

Solution NMR

ANTIFUNGAL PROTEIN FROM STREPTOMYCES TENDAE TU901, 30-CONFORMERS ENSEMBLE

Released:
DOI: 10.2210/pdb1g6e/pdb
PDB entry 1g6e coloured by chain, ensemble of 30 models, front view.
PDB entry 1g6e coloured by chain, ensemble of 30 models, side view.
PDB entry 1g6e coloured by chain, ensemble of 30 models, top view.
Source organism: Streptomyces tendae
Primary publication:
Solution structure, backbone dynamics and chitin binding of the anti-fungal protein from Streptomyces tendae TU901.
Campos-Olivas R, Hörr I, Bormann C, Jung G, Gronenborn AM
J Mol Biol 308 765-82 (2001)
PMID: 11350173

Function and Biology Details

Biochemical function:
  • not assigned
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-193143 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Streptomyces killer toxin-like beta/gamma crystallin domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 87 amino acids
Theoretical weight: 10 KDa
Source organism: Streptomyces tendae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9RCK8 (Residues: 43-128; Coverage: 86%)
Gene name: afp
Sequence domains: Beta/Gamma crystallin
Structure domains: Gamma-B Crystallin; domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this NMR entry.
Refinement method: Torsion angle dynamics with DYANA.
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Streptomyces: The biofactory of secondary metabolites.
Alam et al. (2022)
1 more

2 mentions without citation

Protein aggregation/folding: the role of deterministic singularities of sequence hydrophobicity as determined by nonlinear signal analysis of acylphosphatase and Abeta(1-40).
Zbilut et al. (2003)
1 more