Crystal Structure of a Michaelis Complex between Plasminogen Activator Inhibitor-1 and Urokinase-type Plasminogen Activator. Determined by X-ray diffraction at 2.3 Å resolution. Released 29 Dec 2010.
Explore 3PB1 in 3D Show helices and sheets RCSB PDB PDBe
3PB1 contains 29 α-helices and 41 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 |
|---|---|---|---|
| β-strand | 17 | 1 | 5 |
| β-strand | 20-21 | 2 | 4 |
| α-helix | 24-26 | 3 | |
| β-strand | 30-36 | 7 | 6 |
| α-helix | 37 | 1 | |
| β-strand | 38-48 | 11 | 6 |
| β-strand | 51-54 | 4 | 6 |
| α-helix | 56-58 | 3 | |
| α-helix | 62-63 | 3 | |
| β-strand | 64-68 | 5 | 6 |
| β-strand | 72 | 1 | 7 |
| β-strand | 81-90 | 10 | 6 |
| β-strand | 95-96 | 2 | 8 |
| β-strand | 99-100 | 2 | 8 |
| β-strand | 104-109 | 6 | 6 |
| β-strand | 115 | 1 | 9 |
| β-strand | 118 | 1 | 9 |
| α-helix | 120-121 | 2 | |
| β-strand | 122 | 1 | 4 |
| α-helix | 123-125 | 3 | |
| α-helix | 130-131 | 2 | |
| β-strand | 135-140 | 6 | 4 |
| α-helix | 151-152 | 2 | |
| β-strand | 154 | 1 | 7 |
| β-strand | 156-163 | 8 | 4 |
| α-helix | 165-168 | 4 | |
| α-helix | 173-175 | 3 | |
| β-strand | 180-184 | 5 | 4 |
| β-strand | 189 | 1 | 5 |
| β-strand | 198-203 | 6 | 4 |
| β-strand | 206-215 | 10 | 4 |
| β-strand | 222 | 1 | 10 |
| β-strand | 224 | 1 | 10 |
| β-strand | 226-230 | 5 | 4 |
| α-helix | 231-233 | 3 | |
| α-helix | 235-241 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-25 | 20 | |
| β-strand | 32-34 | 3 | 1 |
| α-helix | 36-47 | 12 | |
| 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 | |
| α-helix | 121 | 1 | |
| β-strand | 122-124 | 3 | 2 |
| α-helix | 129-143 | 15 | |
| α-helix | 153-156 | 4 | |
| 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 | 1 |
| β-strand | 196-214 | 19 | 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 | 256-264 | 9 | |
| β-strand | 267-276 | 10 | 1 |
| β-strand | 278-285 | 8 | 2 |
| α-helix | 287-292 | 6 | |
| α-helix | 297-299 | 3 | |
| β-strand | 319-328 | 10 | 2 |
| β-strand | 345 | 1 | 4 |
| β-strand | 351-353 | 3 | 1 |
| β-strand | 358-364 | 7 | 1 |
| β-strand | 369-376 | 8 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Plasminogen activator inhibitor 1 | I | protein | 379 | Homo sapiens | P05121 (AlphaFold model) |
| Plasminogen activator, urokinase | E | protein | 253 | Homo sapiens | P00749 (AlphaFold model) |
>3PB1_1 Plasminogen activator inhibitor 1 (chains I) VHHPPSYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQA AMGFKIDDKGMAPALRHLYKELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRST VKQVDFSEVERARFIINDWVKTHTKGMISHLLGTGAVQQLTRLVLVNALYFNGQWKTPFP DSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHYYDILELPYHGDTLSMFIAAP YEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFR QFQADFTSLSDQEPLHVALALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIIDRPFLF VVRHNPTGTVLFMGQVMEP
>3PB1_2 Plasminogen activator, urokinase (chains E) IIGGEFTTIENQPWFAAIYRRHRGGSVTYVCGGSLISPCWVISATHCFIDYPKKEDYIVY LGRSRLNSNTQGEMKFEVENLILHKDYSADTLAHHNDIALLKIRSKEGRCAQPSRTIQTI ALPSMYNDPQFGTSCEITGFGKEQSTDYLYPEQLKMTVVKLISHRECQQPHYYGSEVTTK MLCAADPQWKTDSCQGDAGGPLVCSLQGRMTLTGIVSWGRGCALKDKPGVYTRVSHFLPW IRSHTKEENGLAL
Structural basis for recognition of urokinase-type plasminogen activator by plasminogen activator inhibitor-1. Lin, Z., Jiang, L., Yuan, C. et al. J Biol Chem (2011) 286:7027-7032. DOI 10.1074/jbc.M110.204537 · 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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