› 5ile

X-ray diffraction
1.77Å resolution

H64A sperm whale myoglobin with a Fe-tolyl moiety

Released:
DOI: 10.2210/pdb5ile/pdb
PDB entry 5ile coloured by chain, front view.
PDB entry 5ile coloured by chain, side view.
PDB entry 5ile coloured by chain, top view.
Source organism: Physeter catodon
Primary publication:
Organometallic myoglobins: Formation of Fe-carbon bonds and distal pocket effects on aryl ligand conformations.
Wang B, Thomas LM, Richter-Addo GB
J Inorg Biochem 164 1-4 (2016)
PMID: 27687333

Function and Biology Details

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

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: 154 amino acids
Theoretical weight: 17.3 KDa
Source organism: Physeter catodon
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P02185 (Residues: 1-154; Coverage: 100%)
Gene name: MB
Sequence domains: Globin
Structure domains: Globins

Ligands and Environments

2 bound ligands:
Ligand 6CQ 1 x 6CQ
Ligand SO4 6 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P6
Unit cell:
a: 90.794Å b: 90.794Å c: 45.317Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.154 0.153 0.179
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 citation in other articles

Nitrosyl Myoglobins and Their Nitrite Precursors: Crystal Structural and Quantum Mechanics and Molecular Mechanics Theoretical Investigations of Preferred Fe -NO Ligand Orientations in Myoglobin Distal Pockets.
Wang et al. (2018)
1 more

3 mentions without citation

Organometallic myoglobins: Formation of Fe-carbon bonds and distal pocket effects on aryl ligand conformations.
Wang et al. (2016)
2 more