› 1r2m

X-ray diffraction
1Å resolution

Atomic resolution structure of the HFBII hydrophobin: a self-assembling amphiphile

Released:
DOI: 10.2210/pdb1r2m/pdb
PDB entry 1r2m coloured by chain, front view.
PDB entry 1r2m coloured by chain, side view.
PDB entry 1r2m coloured by chain, top view.
Source organism: Trichoderma reesei
Primary publication:
Atomic resolution structure of the HFBII hydrophobin, a self-assembling amphiphile.
Hakanpää J, Paananen A, Askolin S, Nakari-Setälä T, Parkkinen T, Penttilä M, Linder MB, Rouvinen J
J Biol Chem 279 534-9 (2004)
PMID: 14555650

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160309 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hydrophobin-2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 71 amino acids
Theoretical weight: 7.2 KDa
Source organism: Trichoderma reesei
UniProt:
  • Canonical: P79073 (Residues: 16-86; Coverage: 100%)
Gene name: hfb2
Sequence domains: Fungal hydrophobin
Structure domains: Hydrophobin

Ligands and Environments

1 bound ligand:
Ligand MN 1 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: C2
Unit cell:
a: 78.657Å b: 46.31Å c: 34.593Å
α: 90° β: 112.16° γ: 90°
R-values:
R R work R free
0.138 0.137 0.153

Quick links

Citations

14 review citations

The power of two: protein dimerization in biology.
Marianayagam et al. (2004)
13 more

8 mentions without citation

The Diverse Structures and Functions of Surfactant Proteins.
Schor et al. (2016)
7 more