cytoglobin cavities. Determined by X-ray diffraction at 2.4 Å resolution. Released 15 Dec 2004.
Explore 1URY in 3D Show helices and sheets RCSB PDB PDBe
1URY contains 20 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 | 21-35 | 15 | |
| α-helix | 38-52 | 15 | |
| α-helix | 54-59 | 6 | |
| α-helix | 69-72 | 4 | |
| α-helix | 76-94 | 19 | |
| α-helix | 99-111 | 13 | |
| α-helix | 112-116 | 5 | |
| α-helix | 122-138 | 17 | |
| α-helix | 140-142 | 3 | |
| α-helix | 145-169 | 25 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 21-35 | 15 | |
| α-helix | 38-52 | 15 | |
| α-helix | 54-59 | 6 | |
| α-helix | 69-74 | 6 | |
| α-helix | 76-94 | 19 | |
| α-helix | 99-112 | 14 | |
| α-helix | 113-117 | 5 | |
| α-helix | 122-138 | 17 | |
| α-helix | 140-142 | 3 | |
| α-helix | 145-168 | 24 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cytoglobin | A, B | protein | 190 | HOMO SAPIENS | Q8WWM9 (AlphaFold model) |
>1URY_1 CYTOGLOBIN (chains A, B) MEKVPGEMEIERRERSEELSEAERKAVQAMWARLYANSEDVGVAILVRFFVNFPSAKQYF SQFKHMEDPLEMERSPQLRKHASRVMGALNTVVENLHDPDKVSSVLALVGKAHALKHKVE PVYFKILSGVILEVVAEEFASDFPPETQRAWAKLRGLIYSHVTAAYKEVGWVQQVPNATT PPATLPSSGP
| ID | Name | Formula | Copies |
|---|---|---|---|
| FC6 | HEXACYANOFERRATE(3-) | C6 Fe N6 | 2 |
| XE | Xenon | Xe | 7 |
| HEM | Protoporphyrin IX containing FE | C34 H32 Fe N4 O4 | 2 |
Cytoglobin Cavities. de Sanctis, D., Dewilde, S., Pesce, A. et al. Biochem Biophys Res Commun (2004) 316:1217. DOI 10.1016/J.BBRC.2004.03.007 · PubMed
Other PDB entries of the same protein (UniProt Q8WWM9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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