› 2nbh

Solution NMR

Solution structure of the HYD1 hydrophobin from Schizophyllum commune

Released:
DOI: 10.2210/pdb2nbh/pdb
PDB entry 2nbh coloured by chain, ensemble of 20 models, front view.
PDB entry 2nbh coloured by chain, ensemble of 20 models, side view.
PDB entry 2nbh coloured by chain, ensemble of 20 models, top view.
Source organism: Schizophyllum commune H4-8
Primary publication:
Characterization of a Basidiomycota hydrophobin reveals the structural basis for a high-similarity Class I subdivision.
Gandier JA, Langelaan DN, Won A, O'Donnell K, Grondin JL, Spencer HL, Wong P, Tillier E, Yip C, Smith SP, Master ER
Sci Rep 7 45863 (2017)
PMID: 28393921

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112915 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hydrophobin Chain: A
Molecule details ›
Chain: A
Length: 107 amino acids
Theoretical weight: 10.87 KDa
Source organism: Schizophyllum commune H4-8
Expression system: Escherichia coli
UniProt:
  • Canonical: D8QCG9 (Residues: 18-46, 47-114; Coverage: 100%)
Gene names: HYD1, SCHCODRAFT_58269
Sequence domains: Fungal hydrophobin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 93%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Hydrophobins: multifunctional biosurfactants for interface engineering.
Berger et al. (2019)
4 more

2 mentions without citation

Characterization of a Basidiomycota hydrophobin reveals the structural basis for a high-similarity Class I subdivision.
Gandier et al. (2017)
1 more