Crystal structure of the complex of human angiotensinogen and renin at 2.55 Angstrom. Determined by X-ray diffraction at 2.55 Å resolution. Released 26 Dec 2018.
Explore 6I3F in 3D Show helices and sheets RCSB PDB PDBe
6I3F contains 30 α-helices and 54 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 |
|---|---|---|---|
| β-strand | 33-34 | 2 | 1 |
| α-helix | 36-37 | 2 | |
| β-strand | 38 | 1 | 2 |
| α-helix | 44-46 | 3 | |
| α-helix | 48-60 | 13 | |
| α-helix | 64-91 | 28 | |
| β-strand | 98-101 | 4 | 3 |
| α-helix | 103-115 | 13 | |
| α-helix | 119-129 | 11 | |
| α-helix | 144-159 | 16 | |
| β-strand | 170-180 | 11 | 2 |
| β-strand | 186-187 | 2 | 1 |
| α-helix | 188-194 | 7 | |
| β-strand | 201-205 | 5 | 2 |
| α-helix | 211-226 | 16 | |
| α-helix | 234-236 | 3 | |
| β-strand | 243-254 | 12 | 2 |
| β-strand | 258-260 | 3 | 3 |
| β-strand | 265-270 | 6 | 4 |
| β-strand | 273-277 | 5 | 4 |
| β-strand | 279-291 | 13 | 3 |
| β-strand | 296-302 | 7 | 3 |
| β-strand | 307-314 | 8 | 3 |
| α-helix | 317-319 | 3 | |
| α-helix | 320-325 | 6 | |
| α-helix | 328-330 | 3 | |
| α-helix | 334-336 | 3 | |
| β-strand | 340-349 | 10 | 3 |
| β-strand | 352-358 | 7 | 2 |
| α-helix | 359-365 | 7 | |
| β-strand | 388-390 | 3 | 2 |
| β-strand | 392-400 | 9 | 2 |
| β-strand | 419-422 | 4 | 3 |
| β-strand | 427-433 | 7 | 3 |
| α-helix | 434-436 | 3 | |
| β-strand | 438-445 | 8 | 3 |
| α-helix | 452-455 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6 | 1 | 5 |
| β-strand | 8-12 | 5 | 6 |
| β-strand | 13-15 | 3 | 7 |
| β-strand | 19-26 | 8 | 7 |
| β-strand | 31-38 | 8 | 7 |
| β-strand | 44-47 | 4 | 7 |
| β-strand | 48 | 1 | 8 |
| α-helix | 56-59 | 4 | |
| β-strand | 64 | 1 | 8 |
| α-helix | 66-68 | 3 | |
| β-strand | 73-82 | 10 | 7 |
| β-strand | 87-99 | 13 | 7 |
| β-strand | 102-113 | 12 | 7 |
| α-helix | 116-119 | 4 | |
| β-strand | 126-129 | 4 | 7 |
| α-helix | 133-135 | 3 | |
| α-helix | 137-139 | 3 | |
| α-helix | 140-142 | 3 | |
| α-helix | 143-150 | 8 | |
| β-strand | 153 | 1 | 5 |
| β-strand | 157-162 | 6 | 6 |
| β-strand | 174-178 | 5 | 6 |
| β-strand | 186 | 1 | 9 |
| β-strand | 191-194 | 4 | 6 |
| β-strand | 202-205 | 4 | 10 |
| β-strand | 207-210 | 4 | 11 |
| β-strand | 216 | 1 | 11 |
| β-strand | 221-225 | 5 | 10 |
| β-strand | 232-234 | 3 | 10 |
| α-helix | 236-246 | 11 | |
| β-strand | 249-251 | 3 | 12 |
| β-strand | 254-258 | 5 | 12 |
| α-helix | 262-264 | 3 | |
| α-helix | 266-267 | 2 | |
| β-strand | 268-271 | 4 | 11 |
| β-strand | 276-279 | 4 | 11 |
| α-helix | 281-284 | 4 | |
| β-strand | 285 | 1 | 13 |
| β-strand | 295-297 | 3 | 12 |
| β-strand | 298 | 1 | 13 |
| β-strand | 300-302 | 3 | 10 |
| α-helix | 305-306 | 2 | |
| β-strand | 313-315 | 3 | 10 |
| α-helix | 317-320 | 4 | |
| β-strand | 323-328 | 6 | 6 |
| β-strand | 333-338 | 6 | 6 |
| β-strand | 339 | 1 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Angiotensinogen | A | protein | 458 | Homo sapiens | P01019 (AlphaFold model) |
| Renin | B | protein | 340 | Homo sapiens | P00797 (AlphaFold model) |
>6I3F_1 Angiotensinogen (chains A) DRVYIHPFHLVIHNESTCEQLAKANAGKPKDPTFIPAPIQAKTSPVDEKALQDQLVLVAA KLDTEDKLRAAMVGMLANFLGFRIYGMHSELWGVVHGATVLSPTAVFGTLASLYLGALDH TADRLQAILGVPWKDKQCTSRLDAHKVLSALQAVQGLLVAQGRADSQAQLLLSTVVGVFT APGLHLKQPFVQGLALYTPVVLPRSLDFTELDVAAEKIDRFMQAVTGWKTGSSLMGASVD STLAFNTYVHFQGKMKGFSLLAEPQEFWVDQSTSVSVPMLSGMGTFQHWSDIQDQFSVTQ VPFTESASLLLIQPHYASDLDKVEGLTFQQNSLNWMKKLSPRTIHLTMPQLVLQGSYDLQ DLLAQAELPAILHTELNLQKLSNDRIRVGEVLNSIFFELEADEREPTESTQQLNKPEVLE VTLNRPFLFAVYDQSATALHFLGRVANPLSTAHHHHHH
>6I3F_2 Renin (chains B) LTLGNTTSSVILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSNVWVPSSKCSRLYTACVY HKLFDASDSSSYKHNGTELTLRYSTGTVSGFLSQDIITVGGITVTQMFGEVTEMPALPFM LAEFDGVVGMGFIEQAIGRVTPIFDNIISQGVLKEDVFSFYYNRDSENSQSLGGQIVLGG SDPQHYEGNFHYINLIKTGVWQIQMKGVSVGSSTLLCEDGCLALVATGASYISGSTSSIE KLMEALGAKKRLFDYVVKCNEGPTLPDISFHLGGKEYTLTSADYVFQESYSSKKLCTLAI HAMDIPPPTGPTWALGATFIRKFYTEFDRRNNRIGFALAR
Structural basis for the specificity of renin-mediated angiotensinogen cleavage. Yan, Y., Zhou, A., Carrell, R.W. et al. J Biol Chem (2019) 294:2353-2364. DOI 10.1074/jbc.RA118.006608 · 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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