Plasminogen activator inhibitor-1. Determined by X-ray diffraction at 2.6 Å resolution. Released 17 Dec 1999.
Explore 1C5G in 3D Show helices and sheets RCSB PDB PDBe
1C5G contains 14 α-helices and 18 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 | 27-48 | 22 | |
| β-strand | 53 | 1 | 1 |
| β-strand | 56-57 | 2 | 2 |
| α-helix | 59-68 | 10 | |
| α-helix | 75-85 | 11 | |
| α-helix | 94-105 | 12 | |
| α-helix | 108-110 | 3 | |
| β-strand | 113-123 | 11 | 3 |
| α-helix | 128-129 | 2 | |
| α-helix | 132-140 | 9 | |
| β-strand | 145-147 | 3 | 3 |
| α-helix | 152-166 | 15 | |
| α-helix | 177-179 | 3 | |
| β-strand | 186-197 | 12 | 3 |
| β-strand | 198 | 1 | 4 |
| α-helix | 201-203 | 3 | |
| β-strand | 208-211 | 4 | 2 |
| β-strand | 221-238 | 18 | 2 |
| β-strand | 242-250 | 9 | 2 |
| β-strand | 251 | 1 | 4 |
| β-strand | 256-263 | 8 | 2 |
| α-helix | 271-274 | 4 | |
| α-helix | 279-286 | 8 | |
| β-strand | 290-299 | 10 | 2 |
| β-strand | 301-308 | 8 | 3 |
| α-helix | 310-316 | 7 | |
| α-helix | 320-322 | 3 | |
| β-strand | 340-351 | 12 | 3 |
| β-strand | 355-366 | 12 | 3 |
| β-strand | 377 | 1 | 1 |
| β-strand | 380-387 | 8 | 2 |
| β-strand | 392-400 | 9 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Plasminogen activator inhibitor-1 | A | protein | 402 | Homo sapiens | P05121 (AlphaFold model) |
>1C5G_1 PLASMINOGEN ACTIVATOR INHIBITOR-1 (chains A) MQMSPALTCLVLGLALVFGEGSAVHHPPSYVAHLASDFGVRVFQQVAQASKDRNVVFSPY GVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALRHLYKELMGPWNKDEISTTDAI FVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAV DQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPD GHYYDILELPYHGDTLSMFIAAPYEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPK FSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQKVKIEVNESGTVASS STAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP
Engineering of plasminogen activator inhibitor-1 to reduce the rate of latency transition. Tucker, H.M., Mottonen, J., Goldsmith, E.J. et al. Nat Struct Biol (1995) 2:442-445. DOI 10.1038/nsb0695-442 · PubMed
Other PDB entries of the same protein (UniProt P05121 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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