› 1mba

X-ray diffraction
1.6Å resolution

APLYSIA LIMACINA MYOGLOBIN. CRYSTALLOGRAPHIC ANALYSIS AT 1.6 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1mba/pdb
PDB entry 1mba coloured by chain, front view.
PDB entry 1mba coloured by chain, side view.
PDB entry 1mba coloured by chain, top view.
Source organism: Aplysia limacina
Primary publication:
Aplysia limacina myoglobin. Crystallographic analysis at 1.6 A resolution.
Bolognesi M, Onesti S, Gatti G, Coda A, Ascenzi P, Brunori M
J Mol Biol 205 529-44 (1989)
PMID: 2926816

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-135419 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Globin Chain: A
Molecule details ›
Chain: A
Length: 147 amino acids
Theoretical weight: 15.35 KDa
Source organism: Aplysia limacina
Expression system: Not provided
UniProt:
  • Canonical: P02210 (Residues: 2-146; Coverage: 99%)
Sequence domains: Globin
Structure domains: Globins

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 52.98Å b: 70.7Å c: 32.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.193 not available
Expression system: Not provided

Quick links

Citations

6 review citations

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

28 mentions without citation

Evolution, energy landscapes and the paradoxes of protein folding.
Wolynes PG. (2015)
27 more