Catalytic domain of human two-chain tissue plasminogen activator complex of a bis-benzamidine. Determined by X-ray diffraction at 2.9 Å resolution. Released 20 Apr 1999.
Explore 1A5H in 3D Show helices and sheets RCSB PDB PDBe
1A5H contains 23 α-helices and 36 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 | 1 |
| β-strand | 20-21 | 2 | 2 |
| α-helix | 24-26 | 3 | |
| β-strand | 30-35 | 6 | 3 |
| α-helix | 38 | 1 | |
| β-strand | 39-48 | 10 | 3 |
| β-strand | 51-54 | 4 | 3 |
| α-helix | 56-59 | 4 | |
| α-helix | 61-63 | 3 | |
| β-strand | 64-68 | 5 | 3 |
| β-strand | 72 | 1 | 4 |
| β-strand | 81-90 | 10 | 3 |
| β-strand | 104-108 | 5 | 3 |
| α-helix | 109 | 1 | |
| α-helix | 120-121 | 2 | |
| β-strand | 122 | 1 | 2 |
| α-helix | 123-125 | 3 | |
| α-helix | 130-131 | 2 | |
| β-strand | 135-140 | 6 | 2 |
| β-strand | 154 | 1 | 4 |
| β-strand | 156-162 | 7 | 2 |
| α-helix | 163-164 | 2 | |
| α-helix | 169B-171 | 3 | |
| β-strand | 180-184 | 5 | 2 |
| β-strand | 189 | 1 | 1 |
| β-strand | 198-203 | 6 | 2 |
| β-strand | 206-215 | 10 | 2 |
| β-strand | 226-230 | 5 | 2 |
| α-helix | 231-234 | 4 | |
| α-helix | 235-241 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 17 | 1 | 5 |
| β-strand | 20-21 | 2 | 6 |
| α-helix | 24-26 | 3 | |
| β-strand | 30-36 | 7 | 7 |
| β-strand | 38-48 | 11 | 7 |
| β-strand | 51-54 | 4 | 7 |
| α-helix | 56-59 | 4 | |
| α-helix | 61-63 | 3 | |
| β-strand | 64-68 | 5 | 7 |
| β-strand | 72 | 1 | 8 |
| β-strand | 81-90 | 10 | 7 |
| β-strand | 104-108 | 5 | 7 |
| α-helix | 109 | 1 | |
| α-helix | 120-121 | 2 | |
| β-strand | 122 | 1 | 6 |
| α-helix | 123-125 | 3 | |
| α-helix | 130-131 | 2 | |
| β-strand | 135-140 | 6 | 6 |
| β-strand | 154 | 1 | 8 |
| β-strand | 156-162 | 7 | 6 |
| α-helix | 163-164 | 2 | |
| α-helix | 169A-170 | 3 | |
| β-strand | 180-184 | 5 | 6 |
| β-strand | 189 | 1 | 5 |
| β-strand | 198-203 | 6 | 6 |
| β-strand | 206-215 | 10 | 6 |
| β-strand | 226-230 | 5 | 6 |
| α-helix | 231-234 | 4 | |
| α-helix | 235-241 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tissue plasminogen activator | C, D | protein | 7 | Homo sapiens | P00750 (AlphaFold model) |
| Tissue plasminogen activator | A, B | protein | 252 | Homo sapiens | P00750 (AlphaFold model) |
>1A5H_1 TISSUE PLASMINOGEN ACTIVATOR (chains C, D) TCGLRQY
>1A5H_2 TISSUE PLASMINOGEN ACTIVATOR (chains A, B) IKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTV ILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVC LPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNM LCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVT NYLDWIRDNMRP
| ID | Name | Formula | Copies |
|---|---|---|---|
| BBA | 2,7-bis-(4-amidinobenzylidene)-cycloheptan-1-one | C23 H28 N4 O | 2 |
Structural mapping of the active site specificity determinants of human tissue-type plasminogen activator. Implications for the design of low molecular weight substrates and inhibitors. Renatus, M., Bode, W., Huber, R. et al. J Biol Chem (1997) 272:21713-21719. DOI 10.1074/jbc.272.35.21713 · PubMed
Other PDB entries of the same protein (UniProt P00750 (AlphaFold model), which also has an AlphaFold model), best resolution first:
1A5H is part of these collections:
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