Crystal structure of myoglobin reconstituted with 6-methyl-6-depropionatehemin. Determined by X-ray diffraction at 1.1 Å resolution. Released 14 Aug 2007.
Explore 2EKT in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-18 | 15 | |
| α-helix | 21-35 | 15 | |
| α-helix | 37-42 | 6 | |
| α-helix | 52-57 | 6 | |
| α-helix | 59-77 | 19 | |
| α-helix | 83-91 | 9 | |
| α-helix | 92-97 | 6 | |
| α-helix | 101-118 | 18 | |
| α-helix | 125-149 | 25 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Myoglobin | A | protein | 153 | Physeter catodon | P02185 (AlphaFold model) |
>2EKT_1 Myoglobin (chains A) VLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPETLEKFDRFKHLKTEAEMKASED LKKHGVTVLTALGAILKKKGHHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHP GDFGADAQGAMNKALELFRKDIAAKYKELGYQG
| ID | Name | Formula | Copies |
|---|---|---|---|
| 6HE | 6-methy-6-depropionatehemin | C32 H30 Fe N4 O2 | 1 |
Water and common crystallization additives (SO4) are not listed.
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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