› 1bet

X-ray diffraction
2.3Å resolution

NEW PROTEIN FOLD REVEALED BY A 2.3 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF NERVE GROWTH FACTOR

Released:
DOI: 10.2210/pdb1bet/pdb
PDB entry 1bet coloured by chain, front view.
PDB entry 1bet coloured by chain, side view.
PDB entry 1bet coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
New protein fold revealed by a 2.3-A resolution crystal structure of nerve growth factor.
McDonald NQ, Lapatto R, Murray-Rust J, Gunning J, Wlodawer A, Blundell TL
Nature 354 411-4 (1991)
PMID: 1956407

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-134072 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-nerve growth factor Chain: A
Molecule details ›
Chain: A
Length: 107 amino acids
Theoretical weight: 11.99 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
  • Canonical: P01139 (Residues: 131-237; Coverage: 48%)
Gene names: Ngf, Ngfb
Sequence domains: Nerve growth factor family
Structure domains: Cystine-knot cytokines

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P6522
Unit cell:
a: 56.48Å b: 56.48Å c: 182.39Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.22 0.22 not available
Expression system: Not provided

Quick links

Citations

64 review citations

Neurotrophins: roles in neuronal development and function.
Huang et al. (2001)
63 more

23 mentions without citation

Knotted and topologically complex proteins as models for studying folding and stability.
Yeates et al. (2007)
22 more