Crystal structure of human angiotensinogen. Determined by X-ray diffraction at 3.3 Å resolution. Released 20 Oct 2010.
Explore 2WXW in 3D Show helices and sheets RCSB PDB PDBe
2WXW contains 17 α-helices and 26 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 |
|---|---|---|---|
| β-strand | 12 | 1 | 1 |
| α-helix | 15-24 | 10 | |
| β-strand | 33-34 | 2 | 2 |
| α-helix | 35-37 | 3 | |
| β-strand | 38 | 1 | 3 |
| α-helix | 43-46 | 4 | |
| α-helix | 48-60 | 13 | |
| α-helix | 64-84 | 21 | |
| α-helix | 85-87 | 3 | |
| β-strand | 97 | 1 | 4 |
| β-strand | 100-101 | 2 | 5 |
| α-helix | 103-115 | 13 | |
| α-helix | 121-129 | 9 | |
| β-strand | 142 | 1 | 1 |
| α-helix | 144-158 | 15 | |
| β-strand | 170-179 | 10 | 4 |
| α-helix | 180-181 | 2 | |
| β-strand | 186-187 | 2 | 2 |
| α-helix | 188-197 | 10 | |
| β-strand | 201-203 | 3 | 4 |
| β-strand | 205 | 1 | 3 |
| α-helix | 211-226 | 16 | |
| β-strand | 244-255 | 12 | 4 |
| β-strand | 258-260 | 3 | 6 |
| β-strand | 267 | 1 | 7 |
| β-strand | 275 | 1 | 7 |
| β-strand | 280-287 | 8 | 6 |
| β-strand | 288-289 | 2 | 5 |
| β-strand | 296-300 | 5 | 5 |
| β-strand | 303 | 1 | 5 |
| β-strand | 307-314 | 8 | 5 |
| α-helix | 320-325 | 6 | |
| α-helix | 332-335 | 4 | |
| β-strand | 341-348 | 8 | 6 |
| α-helix | 349-351 | 3 | |
| β-strand | 352-358 | 7 | 4 |
| α-helix | 359-362 | 4 | |
| α-helix | 369-373 | 5 | |
| β-strand | 392-401 | 10 | 4 |
| β-strand | 419-422 | 4 | 6 |
| β-strand | 427-433 | 7 | 5 |
| β-strand | 438-439 | 2 | 5 |
| β-strand | 442-445 | 4 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Angiotensinogen | A | protein | 453 | HOMO SAPIENS | P01019 (AlphaFold model) |
>2WXW_1 ANGIOTENSINOGEN (chains A) SDRVYIHPFHLVIHNESTCEQLAKANAGKPKDPTFIPAPIQAKTSPVDEKALQDQLVLVA AKLDTEDKLRAAMVGMLANFLGFRIYGMHSELWGVVHGATVLSPTAVFGTLASLYLGALD HTADRLQAILGVPWKDKNCTSRLDAHKVLSALQAVQGLLVAQGRADSQAQLLLSTVVGVF TAPGLHLKQPFVQGLALYTPVVLPRSLDFTELDVAAEKIDRFMQAVTGWKTGCSLMGASV DSTLAFNTYVHFQGKMKGFSLLAEPQEFWVDNSTSVSVPMLSGMGTFQHWSDIQDNFSVT QVPFTESACLLLIQPHYASDLDKVEGLTFQQNSLNWMKKLSPRTIHLTMPQLVLQGSYDL QDLLAQAELPAILHTELNLQKLSNDRIRVGEVLNSIFFELEADEREPTESTQQLNKPEVL EVTLNRPFLFAVYDQSATALHFLGRVANPLSTA
A Redox Switch in Angiotensinogen Modulates Angiotensin Release. Zhou, A., Carrell, R.W., Murphy, M.P. et al. Nature (2010) 468:108. DOI 10.1038/NATURE09505 · PubMed
Other PDB entries of the same protein (UniProt P01019 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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