Crystal Structure of the Mitochondrial Serine Protease HtrA2. Determined by X-ray diffraction at 2.0 Å resolution. Released 22 May 2002.
Explore 1LCY in 3D Show helices and sheets RCSB PDB PDBe
1LCY contains 12 α-helices and 21 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 |
|---|---|---|---|
| α-helix | 10-13 | 4 | |
| α-helix | 16-24 | 9 | |
| α-helix | 25-27 | 3 | |
| β-strand | 28-37 | 10 | 1 |
| β-strand | 42-55 | 14 | 1 |
| β-strand | 59-62 | 4 | 1 |
| α-helix | 64-67 | 4 | |
| β-strand | 72-76 | 5 | 1 |
| β-strand | 82-91 | 10 | 1 |
| β-strand | 96-100 | 5 | 1 |
| α-helix | 106-108 | 3 | |
| β-strand | 112 | 1 | 2 |
| α-helix | 115-117 | 3 | |
| α-helix | 118-119 | 2 | |
| β-strand | 123-126 | 4 | 2 |
| β-strand | 138-142 | 5 | 2 |
| α-helix | 161 | 1 | |
| β-strand | 162-164 | 3 | 2 |
| β-strand | 176-179 | 4 | 2 |
| β-strand | 184-193 | 10 | 2 |
| β-strand | 196-201 | 6 | 2 |
| α-helix | 202-208 | 7 | |
| β-strand | 227-228 | 2 | 3 |
| β-strand | 231-235 | 5 | 4 |
| α-helix | 238-244 | 7 | |
| β-strand | 258-263 | 6 | 4 |
| α-helix | 268-272 | 5 | |
| β-strand | 279-283 | 5 | 4 |
| β-strand | 286-287 | 2 | 4 |
| α-helix | 291-298 | 8 | |
| β-strand | 304-310 | 7 | 4 |
| β-strand | 313-319 | 7 | 4 |
| β-strand | 322-323 | 2 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| HtrA2 serine protease | A | protein | 325 | Homo sapiens | O43464 (AlphaFold model) |
>1LCY_1 HtrA2 serine protease (chains A) AVPSPPPASPRSQYNFIADVVEKTAPAVVYIEILDRHPFLGREVPISNGSGFVVAADGLI VTNAHVVADRRRVRVRLLSGDTYEAVVTAVDPVADIATLRIQTKEPLPTLPLGRSADVRQ GEFVVAMGSPFALQNTITSGIVSSAQRPARDLGLPQTNVEYIQTDAAIDFGNAGGPLVNL DGEVIGVNTMKVTAGISFAIPSDRLREFLHRGEKKNSSSGISGSQRRYIGVMMLTLSPSI LAELQLREPSFPDVQHGVLIHKVILGSPAHRAGLRPGDVILAIGEQMVQNAEDVYEAVRT QSQLAVQIRRGRETLTLYVTPEVTE
Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi. Li, W., Srinivasula, S.M., Chai, J. et al. Nat Struct Biol (2002) 9:436-441. DOI 10.1038/nsb795 · PubMed
Other PDB entries of the same protein (UniProt O43464 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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