› 1mnj

X-ray diffraction
2.2Å resolution

INTERACTIONS AMONG RESIDUES CD3, E7, E10 AND E11 IN MYOGLOBINS: ATTEMPTS TO SIMULATE THE O2 AND CO BINDING PROPERTIES OF APLYSIA MYOGLOBIN

Released:
DOI: 10.2210/pdb1mnj/pdb
PDB entry 1mnj coloured by chain, front view.
PDB entry 1mnj coloured by chain, side view.
PDB entry 1mnj coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Interactions among residues CD3, E7, E10, and E11 in myoglobins: attempts to simulate the ligand-binding properties of Aplysia myoglobin.
Smerdon SJ, Krzywda S, Brzozowski AM, Davies GJ, Wilkinson AJ, Brancaccio A, Cutruzzolá F, Allocatelli CT, Brunori M, Li T
Biochemistry 34 8715-25 (1995)
PMID: 7612611

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-135413 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Myoglobin Chains: A, B
Molecule details ›
Chains: A, B
Length: 153 amino acids
Theoretical weight: 16.96 KDa
Source organism: Sus scrofa
Expression system: Not provided
UniProt:
  • Canonical: P02189 (Residues: 2-154; Coverage: 99%)
Gene name: MB
Sequence domains: Globin
Structure domains: Globins

Ligands and Environments

1 bound ligand:
Ligand HEM 2 x HEM
No modified residues

Experiments and Validation Details

Entry percentile scores
Unit cell:
a: 124.29Å b: 42.56Å c: 92.45Å
α: 90° β: 92.65° γ: 90°
R-values:
R R work R free
0.162 not available not available
Expression system: Not provided

Quick links

Citations

4 review citations

Nonvertebrate hemoglobins: functions and molecular adaptations.
Weber et al. (2001)
3 more

1 mention without citation

Water stabilizes an alternate turn conformation in horse heart myoglobin.
Bronstein et al. (2023)