Catalytic domain of human single chain tissue plasminogen activator in complex with dansyl-egr-cmk (dansyl-glu-gly-arg chloromethyl ketone). Determined by X-ray diffraction at 3.35 Å resolution. Released 11 May 1999.
Explore 1BDA in 3D Show helices and sheets RCSB PDB PDBe
1BDA contains 20 α-helices and 46 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 | 1 | 1 | 1 |
| β-strand | 15-16 | 2 | 2 |
| β-strand | 19-21 | 3 | 2 |
| α-helix | 24-26 | 3 | |
| β-strand | 30-36 | 7 | 3 |
| β-strand | 38-48 | 11 | 3 |
| β-strand | 51-54 | 4 | 3 |
| α-helix | 57-59 | 3 | |
| α-helix | 61-63 | 3 | |
| β-strand | 64-68 | 5 | 3 |
| β-strand | 72 | 1 | 4 |
| β-strand | 81-90 | 10 | 3 |
| β-strand | 95 | 1 | 5 |
| β-strand | 100 | 1 | 5 |
| β-strand | 104-109 | 6 | 3 |
| α-helix | 113-114 | 2 | |
| β-strand | 120 | 1 | 1 |
| α-helix | 121 | 1 | |
| β-strand | 122 | 1 | 2 |
| α-helix | 123-125 | 3 | |
| β-strand | 135-140 | 6 | 2 |
| β-strand | 143 | 1 | 6 |
| β-strand | 151 | 1 | 6 |
| β-strand | 154 | 1 | 4 |
| β-strand | 156-162 | 7 | 2 |
| α-helix | 163-164 | 2 | |
| α-helix | 165-167 | 3 | |
| β-strand | 180-184 | 5 | 2 |
| 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 | 235-240 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 15-16 | 2 | 7 |
| β-strand | 19-21 | 3 | 7 |
| α-helix | 24-26 | 3 | |
| β-strand | 30-35 | 6 | 8 |
| β-strand | 40-48 | 9 | 8 |
| β-strand | 51-55 | 5 | 8 |
| α-helix | 57-59 | 3 | |
| α-helix | 61-63 | 3 | |
| β-strand | 64-68 | 5 | 8 |
| β-strand | 72 | 1 | 9 |
| β-strand | 81-90 | 10 | 8 |
| β-strand | 95 | 1 | 10 |
| β-strand | 100 | 1 | 10 |
| β-strand | 103-109 | 7 | 8 |
| α-helix | 113-114 | 2 | |
| β-strand | 115 | 1 | 11 |
| β-strand | 118 | 1 | 11 |
| α-helix | 120-121 | 2 | |
| β-strand | 122 | 1 | 7 |
| α-helix | 123-125 | 3 | |
| α-helix | 130-131 | 2 | |
| β-strand | 135-140 | 6 | 7 |
| β-strand | 143 | 1 | 12 |
| β-strand | 151 | 1 | 12 |
| β-strand | 154 | 1 | 9 |
| β-strand | 156-162 | 7 | 7 |
| α-helix | 163-164 | 2 | |
| α-helix | 165-167 | 3 | |
| β-strand | 180-184 | 5 | 7 |
| β-strand | 198-203 | 6 | 7 |
| β-strand | 206-215 | 10 | 7 |
| β-strand | 226-230 | 5 | 7 |
| α-helix | 231-240 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Single chain tissue type plasminogen activator | A, B | protein | 265 | Homo sapiens | P00750 (AlphaFold model) |
>1BDA_1 SINGLE CHAIN TISSUE TYPE PLASMINOGEN ACTIVATOR (chains A, B) TCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAH CFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSS RCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCT SQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGC GQKDVPGVYTKVTNYLDWIRDNMRP
| ID | Name | Formula | Copies |
|---|---|---|---|
| 2Z0 | N-{[5-(dimethylamino)naphthalen-2-yl]sulfonyl}-L-alpha-glutamyl-N-[(1S)-4-{[ami… | C26 H37 Cl N7 O7 S | 2 |
Lysine 156 promotes the anomalous proenzyme activity of tPA: X-ray crystal structure of single-chain human tPA. Renatus, M., Engh, R.A., Stubbs, M.T. et al. EMBO J (1997) 16:4797-4805. DOI 10.1093/emboj/16.16.4797 · PubMed
Other PDB entries of the same protein (UniProt P00750 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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