1U7R: Myoglobin

Crystal structure of Native Sperm Whale myoglobin from low ionic strength enviroment (Form2 ). Determined by X-ray diffraction at 1.15 Å resolution. Released 19 Jul 2005.

Method
X-ray diffraction
Resolution
1.15 Å
Organism
Physeter catodon
Chains
1
Atoms
1,449
Mol. weight
17.92 kDa
Ligands
HEM
Released
19 Jul 2005

Explore 1U7R in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1U7R contains 10 α-helices and 0 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 10 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix4-1714
α-helix18-203
α-helix21-3515
α-helix37-426
α-helix52-576
α-helix59-7618
α-helix83-9513
α-helix101-11818
α-helix120-1223
α-helix125-14824

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
MyoglobinAprotein153Physeter catodonP02185 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1U7R_1 Myoglobin (chains A)
VLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPETLEKFDRFKHLKTEAEMKASED
LKKHGVTVLTALGAILKKKGHHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHP
GDFGADAQGAMNKALELFRKDIAAKYKELGYQG

Ligands and cofactors

IDNameFormulaCopies
HEMProtoporphyrin IX containing FEC34 H32 Fe N4 O41

Water and common crystallization additives (IMD) are not listed.

Primary citation

Sampling of the native conformational ensemble of myoglobin via structures in different crystalline environments. Kondrashov, D.A., Zhang, W., Aranda, R. et al. Proteins (2008) 70:353-362. DOI 10.1002/prot.21499 · PubMed

Other PDB entries of the same protein (UniProt P02185 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 1U7R directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.