Crystal structure of human caspase-1 with a naturally-occurring Arg240->Gln substitution in complex with 3-[2-(2-benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo-pentanoic acid (z-VAD-FMK)

Summary for 3D6F

Related3d6h 3d6m 1sc3
Related PRD IDPRD_000338
DescriptorCaspase-1, N-[(benzyloxy)carbonyl]-L-valyl-N-[(2S)-1-carboxy-4-fluoro-3-oxobutan-2-yl]-L-alaninamide, ... (4 entities in total)
Functional Keywordscatalytic domain, naturally-occurring mutation, apoptosis, hydrolase, protease, thiol protease, zymogen, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm P29466 P29466
Total number of polymer chains3
Total molecular weight30833.82
Rosen-Wolff, A.,Roesler, J.,Romanowski, M.J. (deposition date: 2008-05-19, release date: 2010-03-02, Last modification date: 2012-12-12)
Primary citation
Rosen-Wolff, A.,Romanowski, M.J.,Ritter, L.,Flecks, S.,Quoos, N.,Gramatt, J.,Petzold, C.,Nguyen, H.D.,Gahr, M.,Roesler, J.
Mutated, structurally altered caspase-1 with decreased enzymatic and increased RIP2-meditated inflammatory activity leads to a new type of periodic fever (ICE fever).
To be Published,
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers 0.2393 0.4% 2.1% 8.0%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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PDB entries from 2020-10-21