› 4lpi

X-ray diffraction
1.36Å resolution

A sperm whale myoglobin double mutant L29H/F43Y Mb with a distal hydrogen-bonding network

Released:
DOI: 10.2210/pdb4lpi/pdb
PDB entry 4lpi coloured by chain, front view.
PDB entry 4lpi coloured by chain, side view.
PDB entry 4lpi coloured by chain, top view.
Source organism: Physeter catodon
Primary publication:
How a novel tyrosine-heme cross-link fine-tunes the structure and functions of heme proteins: a direct comparitive study of L29H/F43Y myoglobin.
Yan DJ, Yuan H, Li W, Xiang Y, He B, Nie CM, Wen GB, Lin YW, Tan X
Dalton Trans 44 18815-22 (2015)
PMID: 26458300

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: 17.41 KDa
Source organism: Physeter catodon
Expression system: Escherichia coli
UniProt:
  • Canonical: P02185 (Residues: 1-154; Coverage: 100%)
Gene name: MB
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
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P212121
Unit cell:
a: 39.884Å b: 48.184Å c: 78.458Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.18 0.199
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Biological and Bioinspired Inorganic N-N Bond-Forming Reactions.
Ferousi et al. (2020)
1 more

1 mention without citation

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