Crystal Structure of Human IPS-1 CARD. Determined by X-ray diffraction at 2.1 Å resolution. Released 11 Dec 2007.
Explore 2VGQ in 3D Show helices and sheets RCSB PDB PDBe
2VGQ contains 31 α-helices and 24 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 | 7-10 | 4 | 1 |
| α-helix | 17-31 | 15 | |
| β-strand | 35-38 | 4 | 1 |
| α-helix | 43-51 | 9 | |
| β-strand | 59-63 | 5 | 1 |
| α-helix | 64-66 | 3 | |
| α-helix | 67-72 | 6 | |
| β-strand | 76 | 1 | 2 |
| α-helix | 77-79 | 3 | |
| α-helix | 83-86 | 4 | |
| β-strand | 89 | 1 | 3 |
| α-helix | 91-96 | 6 | |
| β-strand | 98-99 | 2 | 4 |
| β-strand | 102-103 | 2 | 4 |
| β-strand | 106-111 | 6 | 1 |
| β-strand | 114-118 | 5 | 5 |
| β-strand | 128 | 1 | 6 |
| α-helix | 129-131 | 3 | |
| α-helix | 132-141 | 10 | |
| β-strand | 145-147 | 3 | 5 |
| α-helix | 154-163 | 10 | |
| β-strand | 167-172 | 6 | 7 |
| β-strand | 175-182 | 8 | 7 |
| α-helix | 186-200 | 15 | |
| α-helix | 210-218 | 9 | |
| β-strand | 222-227 | 6 | 5 |
| α-helix | 229-231 | 3 | |
| α-helix | 232-238 | 7 | |
| β-strand | 242-245 | 4 | 5 |
| α-helix | 246-248 | 3 | |
| β-strand | 249 | 1 | 6 |
| β-strand | 250 | 1 | 8 |
| β-strand | 253 | 1 | 8 |
| α-helix | 257 | 1 | |
| β-strand | 258-259 | 2 | 9 |
| β-strand | 260-266 | 7 | 1 |
| β-strand | 267 | 1 | 2 |
| α-helix | 273-279 | 7 | |
| α-helix | 280-284 | 5 | |
| α-helix | 287-296 | 10 | |
| β-strand | 301-302 | 2 | 1 |
| β-strand | 304 | 1 | 3 |
| α-helix | 305-311 | 7 | |
| α-helix | 315-326 | 12 | |
| β-strand | 328-329 | 2 | 9 |
| α-helix | 330-331 | 2 | |
| α-helix | 336-352 | 17 | |
| α-helix | 357-383 | 27 | |
| α-helix | 385-388 | 4 | |
| α-helix | 393-396 | 4 | |
| α-helix | 397-399 | 3 | |
| α-helix | 405-418 | 14 | |
| α-helix | 420-431 | 12 | |
| α-helix | 437-447 | 11 | |
| α-helix | 451-461 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sugar ABC transporter substrate-binding protein,Mitochondrial antiviral-signaling protein | A | protein | 477 | Escherichia coli, Homo sapiens | P0AEX9 (AlphaFold model), Q7Z434 (AlphaFold model) |
>2VGQ_1 Sugar ABC transporter substrate-binding protein,Mitochondrial antiviral-signaling protein (chains A) MKYYHHHHHHDYDHMKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEE KFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIA YPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADG GYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMT INGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLL TDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRT AVINAASGRQTVDEALKDAQTNSAMAFAEDKTYKYICRNFSNFCNVDVVEILPYLPCLTA RDQDRLRATCTLSGNRDTLWHLFNTLQRRPGWVEYFIAALRGCELVDLADEVASVYQ
Crystal Structure of Human Ips-1 Caspase Activation Recruitment Domain. Potter, J.A., Randall, R.E., Taylor, G.L. BMC Struct Biol (2008) 8:11. DOI 10.1186/1472-6807-8-11 · PubMed
Other PDB entries of the same protein (UniProt P0AEX9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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