PDBsum entry 4fc1

Unknown function

PDB id: 4fc1

Contents

Protein chain

46 a.a.

Ligands

DOD ×42

PDB id:

4fc1

Name:

Unknown function

Title:

Ultra-high resolution neutron structure of crambin at room-temperature

Structure:

Crambin. Chain: a

Source:

Crambe hispanica subsp. Abyssinica. Abyssinian crambe,abyssinian kale. Organism_taxid: 3721

Authors:

A.Y.Kovalevsky,J.C.-H.Chen

Key ref:

J.C.Chen et al. (2012). Direct observation of hydrogen atom dynamics and interactions by ultrahigh resolution neutron protein crystallography. Proc Natl Acad Sci U S A, 109, 15301-15306. PubMed id: 22949690

Date:

23-May-12 Release date: 19-Sep-12

Protein chain

P01542  (CRAM_CRAAB) -  Crambin from Crambe hispanica subsp. abyssinica

Seq: 46 a.a.

Struc: 46 a.a.

Proc Natl Acad Sci U S A 109:15301-15306 (2012)

PubMed id: 22949690

Direct observation of hydrogen atom dynamics and interactions by ultrahigh resolution neutron protein crystallography.

J.C.Chen, B.L.Hanson, S.Z.Fisher, P.Langan, A.Y.Kovalevsky.

ABSTRACT

The 1.1 Å, ultrahigh resolution neutron structure of hydrogen/deuterium (H/D) exchanged crambin is reported. Two hundred ninety-nine out of 315, or 94.9%, of the hydrogen atom positions in the protein have been experimentally derived and resolved through nuclear density maps. A number of unconventional interactions are clearly defined, including a potential O─H…π interaction between a water molecule and the aromatic ring of residue Y44, as well as a number of potential C─H…O hydrogen bonds. Hydrogen bonding networks that are ambiguous in the 0.85 Å ultrahigh resolution X-ray structure can be resolved by accurate orientation of water molecules. Furthermore, the high resolution of the reported structure has allowed for the anisotropic description of 36 deuterium atoms in the protein. The visibility of hydrogen and deuterium atoms in the nuclear density maps is discussed in relation to the resolution of the neutron data.