Wild-type human neuroglobin. Determined by X-ray diffraction at 1.74 Å resolution. Released 15 Jan 2014.
Explore 4MPM in 3D Show helices and sheets RCSB PDB PDBe
4MPM contains 22 α-helices and 0 β-strands across 2 chains. 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 | 6-13 | 8 | |
| α-helix | 20-34 | 15 | |
| α-helix | 38-49 | 12 | |
| α-helix | 55-57 | 3 | |
| α-helix | 59-77 | 19 | |
| α-helix | 79-85 | 7 | |
| α-helix | 86-98 | 13 | |
| α-helix | 105-121 | 17 | |
| α-helix | 122-124 | 3 | |
| α-helix | 127-144 | 18 | |
| α-helix | 145-148 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-16 | 11 | |
| α-helix | 20-34 | 15 | |
| α-helix | 36-42 | 7 | |
| α-helix | 52-57 | 6 | |
| α-helix | 59-77 | 19 | |
| α-helix | 79-85 | 7 | |
| α-helix | 86-99 | 14 | |
| α-helix | 105-121 | 17 | |
| α-helix | 122-124 | 3 | |
| α-helix | 127-145 | 19 | |
| α-helix | 146-148 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Neuroglobin | A, B | protein | 151 | Homo sapiens | Q9NPG2 (AlphaFold model) |
>4MPM_1 Neuroglobin (chains A, B) MERPEPELIRQSWRAVSRSPLEHGTVLFARLFALEPDLLPLFQYNCRQFSSPEDCLSSPE FLDHIRKVMLVIDAAVTNVEDLSSLEEYLASLGRKHRAVGVKLSSFSTVGESLLYMLEKC LGPAFTPATRAAWSQLYGAVVQAMSRGWDGE
| ID | Name | Formula | Copies |
|---|---|---|---|
| HEM | Protoporphyrin IX containing FE | C34 H32 Fe N4 O4 | 2 |
The crystal structure of wild-type human brain neuroglobin reveals flexibility of the disulfide bond that regulates oxygen affinity. Guimaraes, B.G., Hamdane, D., Lechauve, C. et al. Acta Crystallogr D Biol Crystallogr (2014) 70:1005-1014. DOI 10.1107/S1399004714000078 · PubMed
Other PDB entries of the same protein (UniProt Q9NPG2 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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