Deoxygenated structure of a distal site hemoglobin mutant plus xe. Determined by X-ray diffraction at 1.07 Å resolution. Released 28 Apr 2009.
Explore 2W72 in 3D Show helices and sheets RCSB PDB PDBe
2W72 contains 40 α-helices and 0 β-strands across 4 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 | 4-17 | 14 | |
| α-helix | 18-20 | 3 | |
| α-helix | 21-35 | 15 | |
| α-helix | 37-42 | 6 | |
| α-helix | 53-71 | 19 | |
| α-helix | 76-79 | 4 | |
| α-helix | 81-86 | 6 | |
| α-helix | 87-91 | 5 | |
| α-helix | 96-112 | 17 | |
| α-helix | 119-137 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-16 | 12 | |
| α-helix | 20-34 | 15 | |
| α-helix | 36-41 | 6 | |
| α-helix | 51-56 | 6 | |
| α-helix | 58-74 | 17 | |
| α-helix | 81-94 | 14 | |
| α-helix | 101-118 | 18 | |
| α-helix | 119-121 | 3 | |
| α-helix | 124-142 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-15 | 11 | |
| α-helix | 20-34 | 15 | |
| α-helix | 36-41 | 6 | |
| α-helix | 43-45 | 3 | |
| α-helix | 51-56 | 6 | |
| α-helix | 58-74 | 17 | |
| α-helix | 75-77 | 3 | |
| α-helix | 81-94 | 14 | |
| α-helix | 101-118 | 18 | |
| α-helix | 119-121 | 3 | |
| α-helix | 124-142 | 19 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Human hemoglobin a | A | protein | 141 | HOMO SAPIENS | P69905 (AlphaFold model) |
| Human hemoglobin a | B, D | protein | 146 | HOMO SAPIENS | P68871 (AlphaFold model) |
| Human hemoglobin a | C | protein | 141 | HOMO SAPIENS | P69905 (AlphaFold model) |
>2W72_1 HUMAN HEMOGLOBIN A (chains A) VLSPADKTNVKAAWGKVGAHAGEYGAEAYERMFLSFPTTKTYFPHFDLSHGSAQVKGQGK KVADALTNAVAHVDDMPNALSALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPA VHASLDKFLASVSTVLTSKYR
>2W72_2 HUMAN HEMOGLOBIN A (chains B, D) MHLTPEEKSAVTALWGKVNVDEVGGEAYGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKV KAQGKKVLGAFSDGLAHLDNLKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGK EFTPPVQAAYQKVVAGVANALAHKYH
>2W72_3 HUMAN HEMOGLOBIN A (chains C) MLSPADKTNVKAAWGKVGAHAGEYGAEAYERMFLSFPTTKTYFPHFDLSHGSAQVKGQGK KVADALTNAVAHVDDMPNALSALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPA VHASLDKFLASVSTVLTSKYR
| ID | Name | Formula | Copies |
|---|---|---|---|
| HEM | Protoporphyrin IX containing FE | C34 H32 Fe N4 O4 | 4 |
| XE | Xenon | Xe | 15 |
| PO4 | Phosphate ion | O4 P | 1 |
Water and common crystallization additives (SO4, K) are not listed.
Pattern of Cavities in Globins: The Case of Human Hemoglobin. Savino, C., Miele, A.E., Draghi, F. et al. Biopolymers (2009) 91:1097. DOI 10.1002/BIP.21201 · PubMed
Other PDB entries of the same protein (UniProt P69905 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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