2EKT: Myoglobin

Crystal structure of myoglobin reconstituted with 6-methyl-6-depropionatehemin. Determined by X-ray diffraction at 1.1 Å resolution. Released 14 Aug 2007.

Method
X-ray diffraction
Resolution
1.1 Å
Organism
Physeter catodon
Chains
1
Atoms
1,626
Mol. weight
18.18 kDa
Ligands
6HE
Released
14 Aug 2007

Explore 2EKT in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2EKT contains 9 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: 9 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix4-1815
α-helix21-3515
α-helix37-426
α-helix52-576
α-helix59-7719
α-helix83-919
α-helix92-976
α-helix101-11818
α-helix125-14925

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
MyoglobinAprotein153Physeter catodonP02185 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2EKT_1 Myoglobin (chains A)
VLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPETLEKFDRFKHLKTEAEMKASED
LKKHGVTVLTALGAILKKKGHHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHP
GDFGADAQGAMNKALELFRKDIAAKYKELGYQG

Ligands and cofactors

IDNameFormulaCopies
6HE6-methy-6-depropionateheminC32 H30 Fe N4 O21

Water and common crystallization additives (SO4) are not listed.

Primary citation

Structure and ligand binding properties of myoglobins reconstituted with monodepropionated heme: functional role of each heme propionate side chain. Harada, K., Makino, M., Sugimoto, H. et al. Biochemistry (2007) 46:9406-9416. DOI 10.1021/bi7007068 · PubMed

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

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