› 1cq2

Neutron Diffraction
2Å resolution

NEUTRON STRUCTURE OF FULLY DEUTERATED SPERM WHALE MYOGLOBIN AT 2.0 ANGSTROM

Released:
DOI: 10.2210/pdb1cq2/pdb
PDB entry 1cq2 coloured by chain, front view.
PDB entry 1cq2 coloured by chain, side view.
PDB entry 1cq2 coloured by chain, top view.
Source organism: Physeter catodon
Primary publication:
Enhanced visibility of hydrogen atoms by neutron crystallography on fully deuterated myoglobin.
Shu F, Ramakrishnan V, Schoenborn BP
Proc Natl Acad Sci U S A 97 3872-7 (2000)
PMID: 10725379

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-135409 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Myoglobin Chain: A
Molecule details ›
Chain: A
Length: 153 amino acids
Theoretical weight: 17.23 KDa
Source organism: Physeter catodon
Expression system: Escherichia coli
UniProt:
  • Canonical: P02185 (Residues: 2-154; Coverage: 99%)
Gene name: MB
Sequence domains: Globin
Structure domains: Globins

Ligands and Environments

2 bound ligands:
Ligand HEM 1 x HEM
Ligand DOD 69 x DOD
No modified residues

Experiments and Validation Details

Spacegroup: P21
Unit cell:
a: 64.53Å b: 30.91Å c: 34.78Å α: 90° β: 105.82° γ: 90°
R-values:
R R work R free 0.16 0.16 0.25
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Challenges and opportunities in cryo-EM single-particle analysis.
Lyumkis D. (2019)
6 more

12 mentions without citation

Evaluation of models determined by neutron diffraction and proposed improvements to their validation and deposition.
Liebschner et al. (2018)
11 more