Allosteric activation of human prekallikrein by apple domain disc rotation. Determined by X-ray diffraction at 1.36 Å resolution. Released 6 Mar 2019.
Explore 6I44 in 3D Show helices and sheets RCSB PDB PDBe
6I44 contains 21 α-helices and 45 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 |
|---|---|---|---|
| β-strand | 6-12 | 7 | 1 |
| β-strand | 16-21 | 6 | 1 |
| α-helix | 25-34 | 10 | |
| β-strand | 40-44 | 5 | 1 |
| α-helix | 46-48 | 3 | |
| β-strand | 57-61 | 5 | 1 |
| β-strand | 70-80 | 11 | 1 |
| α-helix | 86-88 | 3 | |
| β-strand | 97-103 | 7 | 2 |
| β-strand | 105-111 | 7 | 2 |
| α-helix | 115-123 | 9 | |
| β-strand | 130-134 | 5 | 2 |
| α-helix | 141-143 | 3 | |
| β-strand | 146-151 | 6 | 2 |
| α-helix | 153-155 | 3 | |
| β-strand | 159-170 | 12 | 2 |
| α-helix | 173-175 | 3 | |
| β-strand | 187-191 | 5 | 3 |
| β-strand | 195-201 | 7 | 3 |
| α-helix | 205-214 | 10 | |
| β-strand | 220-224 | 5 | 3 |
| α-helix | 231-233 | 3 | |
| β-strand | 236-241 | 6 | 3 |
| β-strand | 251-260 | 10 | 3 |
| β-strand | 278-279 | 2 | 4 |
| β-strand | 282-283 | 2 | 5 |
| β-strand | 286-293 | 8 | 4 |
| α-helix | 296-305 | 10 | |
| β-strand | 311-315 | 5 | 4 |
| α-helix | 318-320 | 3 | |
| β-strand | 321 | 1 | 4 |
| β-strand | 326-332 | 7 | 4 |
| β-strand | 341-342 | 2 | 5 |
| β-strand | 347-351 | 5 | 4 |
| β-strand | 373 | 1 | 6 |
| β-strand | 376-377 | 2 | 7 |
| β-strand | 386-392 | 7 | 8 |
| β-strand | 396-406 | 11 | 8 |
| β-strand | 409-412 | 4 | 8 |
| α-helix | 414-417 | 4 | |
| α-helix | 423-425 | 3 | |
| β-strand | 426-429 | 4 | 8 |
| β-strand | 434 | 1 | 9 |
| α-helix | 435-437 | 3 | |
| β-strand | 445 | 1 | 8 |
| β-strand | 447-452 | 6 | 8 |
| β-strand | 466-470 | 5 | 8 |
| α-helix | 473-476 | 4 | |
| β-strand | 477 | 1 | 10 |
| β-strand | 480 | 1 | 10 |
| α-helix | 482-483 | 2 | |
| β-strand | 484 | 1 | 7 |
| α-helix | 485-486 | 2 | |
| β-strand | 498-502 | 5 | 7 |
| β-strand | 515 | 1 | 9 |
| α-helix | 516 | 1 | |
| β-strand | 517-520 | 4 | 7 |
| β-strand | 523-524 | 2 | 7 |
| α-helix | 526-532 | 7 | |
| β-strand | 542-545 | 4 | 7 |
| β-strand | 553 | 1 | 6 |
| β-strand | 562-567 | 6 | 7 |
| β-strand | 570-579 | 10 | 7 |
| β-strand | 590-594 | 5 | 7 |
| α-helix | 595-598 | 4 | |
| α-helix | 599-609 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Plasma kallikrein | A | protein | 627 | Homo sapiens | P03952 (AlphaFold model) |
>6I44_1 Plasma kallikrein (chains A) RSHHHHHHGCLTQLYENAFFRGGDVASMYTPNAQYCQMRCTFHPRCLLFSFLPASSINDM EKRFGCFLKDSVTGTLPKVHRTGAVSGHSLKQCGHQISACHRDIYKGVDMRGVNFNVSKV SSVEECQKRCTNNIRCQFFSYATQTFHKAEYRNNCLLKYSPGGTPTAIKVLSNVESGFSL KPCALSEIGCHMNIFQHLAFSDVDVARVLTPDAFVCRTICTYHPNCLFFTFYTNVWKIES QRNVCLLKTSESGTPSSSTPQENTISGYSLLTCKRTLPEPCHSKIYPGVDFGGEELNVTF VKGVNVCQETCTKMIRCQFFTYSLLPEDCKAEACKCFLRLSMDGSPTRIAYGTQGSSGYS LRLCNTGDNSVCTTKTSTRIVGGTQSSWGEWPWQVSLQVKLTAQRHLCGGSLIGHQWVLT AAHCFDGLPLQDVWRIYSGILQLSDITKDTPFSQIKEIIIHQNYKVSEGNHDIALIKLQA PLQYTEFQKPICLPSKGDTSTIYTNCWVTGWGFSAEAGEIQNILQKVNIPLVTNEECQKR YQDYKITQRMVCAGYKEGGKDACKGDAGGPLVCKHNGMWRLVGITSWGEGCARREQPGVY TKVAEYMDWILEKTQSSDGKAQMQSPA
| ID | Name | Formula | Copies |
|---|---|---|---|
| BEN | Benzamidine | C7 H8 N2 | 1 |
| PE4 | 2-{2-[2-(2-{2-[2-(2-ethoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethoxy]-ethoxy}-etha… | C16 H34 O8 | 1 |
| GLY | Glycine | C2 H5 N O2 | 1 |
| SER | Serine | C3 H7 N O3 | 1 |
Water and common crystallization additives (MPD, SO4, CL, NA, PEG, GOL, FMT, ACT) are not listed.
Plasma kallikrein structure reveals apple domain disc rotated conformation compared to factor XI. Li, C., Voos, K.M., Pathak, M. et al. J Thromb Haemost (2019) 17:759-770. DOI 10.1111/jth.14418 · PubMed
Other PDB entries of the same protein (UniProt P03952 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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