Crystal structure of the VMA1-derived endonuclease bearing the N and C extein propeptides. Determined by X-ray diffraction at 2.1 Å resolution. Released 29 Aug 2002.
Explore 1JVA in 3D Show helices and sheets RCSB PDB PDBe
1JVA contains 31 α-helices and 67 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 | 285-286 | 2 | 1 |
| β-strand | 290-292 | 3 | 2 |
| β-strand | 293 | 1 | 3 |
| β-strand | 298-300 | 3 | 2 |
| α-helix | 301-303 | 3 | |
| β-strand | 309-311 | 3 | 3 |
| α-helix | 312 | 1 | |
| β-strand | 317-319 | 3 | 3 |
| β-strand | 322 | 1 | 4 |
| β-strand | 325-335 | 11 | 1 |
| β-strand | 355-359 | 5 | 1 |
| β-strand | 363-369 | 7 | 5 |
| β-strand | 372-379 | 8 | 6 |
| β-strand | 382-396 | 15 | 6 |
| β-strand | 402-414 | 13 | 6 |
| α-helix | 415-417 | 3 | |
| α-helix | 420-430 | 11 | |
| β-strand | 437-443 | 7 | 5 |
| α-helix | 444-449 | 6 | |
| α-helix | 452-457 | 6 | |
| β-strand | 459 | 1 | 5 |
| β-strand | 460-462 | 3 | 7 |
| α-helix | 471-478 | 8 | |
| α-helix | 487-501 | 15 | |
| β-strand | 502 | 1 | 8 |
| β-strand | 508-512 | 5 | 8 |
| α-helix | 516-528 | 13 | |
| β-strand | 532-534 | 3 | 8 |
| β-strand | 544-550 | 7 | 8 |
| α-helix | 568-572 | 5 | |
| α-helix | 573-577 | 5 | |
| β-strand | 579-580 | 2 | 9 |
| β-strand | 583-584 | 2 | 9 |
| α-helix | 588-592 | 5 | |
| α-helix | 595-609 | 15 | |
| β-strand | 610-613 | 4 | 10 |
| β-strand | 615 | 1 | 11 |
| β-strand | 617 | 1 | 11 |
| β-strand | 619-624 | 6 | 10 |
| α-helix | 627-640 | 14 | |
| β-strand | 643-649 | 7 | 10 |
| β-strand | 663-669 | 7 | 10 |
| α-helix | 672-678 | 7 | |
| β-strand | 700-702 | 3 | 7 |
| β-strand | 704-715 | 12 | 1 |
| β-strand | 718 | 1 | 4 |
| β-strand | 726-728 | 3 | 12 |
| β-strand | 729 | 1 | 2 |
| β-strand | 733 | 1 | 7 |
| β-strand | 734-736 | 3 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 282 | 1 | 13 |
| β-strand | 285-286 | 2 | 14 |
| β-strand | 290-292 | 3 | 15 |
| β-strand | 293 | 1 | 16 |
| β-strand | 298-300 | 3 | 15 |
| α-helix | 301-303 | 3 | |
| β-strand | 309-311 | 3 | 16 |
| α-helix | 312 | 1 | |
| β-strand | 317-319 | 3 | 16 |
| β-strand | 320-322 | 3 | 17 |
| β-strand | 325-335 | 11 | 14 |
| β-strand | 355-359 | 5 | 14 |
| α-helix | 362 | 1 | |
| β-strand | 363-369 | 7 | 18 |
| β-strand | 371-378 | 8 | 19 |
| β-strand | 383-396 | 14 | 19 |
| β-strand | 402-414 | 13 | 19 |
| α-helix | 415-417 | 3 | |
| α-helix | 420-430 | 11 | |
| β-strand | 437-443 | 7 | 18 |
| α-helix | 444-449 | 6 | |
| α-helix | 452-457 | 6 | |
| β-strand | 459-462 | 4 | 18 |
| α-helix | 471-477 | 7 | |
| α-helix | 487-501 | 15 | |
| β-strand | 508-512 | 5 | 20 |
| α-helix | 516-528 | 13 | |
| β-strand | 532-535 | 4 | 20 |
| β-strand | 544-550 | 7 | 20 |
| α-helix | 568-575 | 8 | |
| β-strand | 579-580 | 2 | 21 |
| β-strand | 583-584 | 2 | 21 |
| α-helix | 589-592 | 4 | |
| α-helix | 595-609 | 15 | |
| β-strand | 610-613 | 4 | 22 |
| β-strand | 619-624 | 6 | 22 |
| α-helix | 627-639 | 13 | |
| β-strand | 643-649 | 7 | 22 |
| β-strand | 663-669 | 7 | 22 |
| α-helix | 672-678 | 7 | |
| β-strand | 700-702 | 3 | 18 |
| β-strand | 704-715 | 12 | 14 |
| β-strand | 718-719 | 2 | 17 |
| α-helix | 720 | 1 | |
| β-strand | 726-728 | 3 | 18 |
| β-strand | 729 | 1 | 15 |
| β-strand | 733-736 | 4 | 18 |
| β-strand | 740 | 1 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| VMA1-derived homing endonuclease X10SSS | A, B | protein | 475 | Saccharomyces cerevisiae | P17255 (AlphaFold model) |
>1JVA_1 VMA1-DERIVED HOMING ENDONUCLEASE X10SSS (chains A, B) MSNSDAIIYVGSFAKGTNVLMADGSIECIENIEVGNKVMGKDGRPREVIKLPRGRETMYS VVQKSQHRAHKSDSSREVPELLKFTCNATNELVVRTPRSVRRLSRTIKGVEYFEVITFEM GQKKAPDGRIVELVKEVSKSYPISEGPERANELVESYRKASNKAYFEWTIEARDLSLLGS HVRKATYQTYAPILYENDHFFDYMQKSKFHLTIEGPKVLAYLLGLWIGDGLSDRATFSVD SRDTSLMERVTEYAEKLNLCAEYKDRKEPQVAKTVNLYSKVVRGNGIRNNLNTENPLWDA IVGLGFLKDGVKNIPSFLSTDNIGTRETFLAGLIDSDGYVTDEHGIKATIKTIHTSVRDG LVSLARSLGLVVSVNAEPAKVDMNGTKHKISYAIYMSGGDVLLNVLSKCAGSKKFRPAPA AAFARECRGFYFELQELKEDDYYGITLSDDSDHQFLLANQVVVHSSGERGNEMAE
Protein-splicing reaction via a thiazolidine intermediate: crystal structure of the VMA1-derived endonuclease bearing the N and C-terminal propeptides. Mizutani, R., Nogami, S., Kawasaki, M. et al. J Mol Biol (2002) 316:919-929. DOI 10.1006/jmbi.2001.5357 · PubMed
Other PDB entries of the same protein (UniProt P17255 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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