plasminogen activator inhibitor-1 complex with somatomedin B domain of vitronectin. Determined by X-ray diffraction at 2.28 Å resolution. Released 19 Jun 2003.
Explore 1OC0 in 3D Show helices and sheets RCSB PDB PDBe
1OC0 contains 17 α-helices and 19 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 |
|---|---|---|---|
| α-helix | 7-25 | 19 | |
| β-strand | 32-34 | 3 | 1 |
| α-helix | 36-49 | 14 | |
| α-helix | 52-62 | 11 | |
| α-helix | 71-82 | 12 | |
| β-strand | 91-100 | 10 | 2 |
| α-helix | 104-106 | 3 | |
| α-helix | 109-117 | 9 | |
| β-strand | 122-124 | 3 | 2 |
| α-helix | 129-142 | 14 | |
| β-strand | 163-172 | 10 | 2 |
| α-helix | 173-174 | 2 | |
| β-strand | 175 | 1 | 3 |
| α-helix | 178-180 | 3 | |
| α-helix | 181-183 | 3 | |
| β-strand | 185-190 | 6 | 4 |
| β-strand | 196-208 | 13 | 4 |
| β-strand | 210-214 | 5 | 1 |
| β-strand | 220-227 | 8 | 1 |
| β-strand | 228 | 1 | 3 |
| α-helix | 229-231 | 3 | |
| β-strand | 233-240 | 8 | 1 |
| α-helix | 248-251 | 4 | |
| α-helix | 256-260 | 5 | |
| β-strand | 269-276 | 8 | 4 |
| β-strand | 278-285 | 8 | 2 |
| α-helix | 287-292 | 6 | |
| α-helix | 297-299 | 3 | |
| β-strand | 319-328 | 10 | 2 |
| β-strand | 351-353 | 3 | 4 |
| β-strand | 358-364 | 7 | 1 |
| β-strand | 369-376 | 8 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 20 | 1 | 5 |
| α-helix | 25-28 | 4 | |
| β-strand | 31 | 1 | 5 |
| α-helix | 35-38 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Plasminogen activator inhibitor-1 | A | protein | 379 | HOMO SAPIENS | P05121 (AlphaFold model) |
| Vitronectin | B | protein | 51 | HOMO SAPIENS | P04004 (AlphaFold model) |
>1OC0_1 PLASMINOGEN ACTIVATOR INHIBITOR-1 (chains A) VHHPPSYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQA AMGFKIDDKGMAPALRHLYKELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRST VKQVDFSEVERARFIINDWVKTHTKGMISHLLGTGAVDQLTRLVLVNALYFNGQWKTPFP DSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHYYDILELPYHGDTLSMFIAAP YEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFR QFQADFTSLSDQEPLHVALALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIIDRPFLF VVRHNPTGTVLFMGQVMEP
>1OC0_2 VITRONECTIN (chains B) DQESCKGRCTEGFNVDKKCQCDELCSYYQSCCTDYTAECKPQVTRGDVFTM
How Vitronectin Binds Pai-1 to Modulate Fibrinolysis and Cell Migration. Zhou, A., Huntington, J.A., Pannu, N.S. et al. Nat Struct Biol (2003) 10:541. DOI 10.1038/NSB943 · 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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