Structure of Human Neurolysin in complex with dynorphin A13 peptide. Determined by X-ray diffraction at 1.99 Å resolution. Released 21 Aug 2024.
Explore 8VJU in 3D Show helices and sheets RCSB PDB PDBe
8VJU contains 44 α-helices and 15 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 |
|---|---|---|---|
| α-helix | 31-54 | 24 | |
| α-helix | 62-67 | 6 | |
| α-helix | 68-84 | 17 | |
| α-helix | 86-88 | 3 | |
| α-helix | 93-114 | 22 | |
| α-helix | 117-129 | 13 | |
| α-helix | 132-134 | 3 | |
| α-helix | 137-152 | 16 | |
| α-helix | 159-184 | 26 | |
| β-strand | 189-192 | 4 | 1 |
| α-helix | 195-197 | 3 | |
| α-helix | 202-205 | 4 | |
| β-strand | 209-210 | 2 | 1 |
| β-strand | 216-219 | 4 | 1 |
| α-helix | 222-231 | 10 | |
| α-helix | 235-245 | 11 | |
| α-helix | 250-271 | 22 | |
| α-helix | 276-281 | 6 | |
| α-helix | 289-325 | 37 | |
| α-helix | 335-337 | 3 | |
| α-helix | 338-350 | 13 | |
| α-helix | 354-357 | 4 | |
| α-helix | 358-360 | 3 | |
| β-strand | 362 | 1 | 2 |
| α-helix | 363-378 | 16 | |
| β-strand | 380-384 | 5 | 3 |
| α-helix | 385 | 1 | |
| β-strand | 396-402 | 7 | 3 |
| β-strand | 408-415 | 8 | 3 |
| β-strand | 427-432 | 6 | 3 |
| β-strand | 435 | 1 | 4 |
| β-strand | 436 | 1 | 5 |
| β-strand | 442 | 1 | 5 |
| α-helix | 443-444 | 2 | |
| β-strand | 445-450 | 6 | 3 |
| α-helix | 453-456 | 4 | |
| β-strand | 463 | 1 | 2 |
| α-helix | 466-484 | 19 | |
| β-strand | 487 | 1 | 4 |
| α-helix | 490-492 | 3 | |
| α-helix | 503-510 | 8 | |
| α-helix | 511-513 | 3 | |
| α-helix | 516-522 | 7 | |
| α-helix | 530-533 | 4 | |
| α-helix | 534-542 | 9 | |
| α-helix | 543-545 | 3 | |
| α-helix | 548-565 | 18 | |
| α-helix | 573-580 | 8 | |
| α-helix | 581-585 | 5 | |
| α-helix | 588-590 | 3 | |
| α-helix | 595-598 | 4 | |
| α-helix | 600-603 | 4 | |
| α-helix | 612-623 | 12 | |
| α-helix | 624-629 | 6 | |
| α-helix | 636-642 | 7 | |
| α-helix | 643-647 | 5 | |
| α-helix | 655-663 | 9 | |
| α-helix | 670-674 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-6 | 2 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Neurolysin, mitochondrial | A | protein | 667 | Homo sapiens | Q9BYT8 (AlphaFold model) |
| Dynorphin A(1-13) | C | protein | 13 | Homo sapiens | P01213 (AlphaFold model) |
>8VJU_1 Neurolysin, mitochondrial (chains A) SSYTVAGRNVLRWDLSPEQIKTRTEELIVQTKQVYDAVGMLGIEEVTYENCLQALADVEV KYIVERTMLDFPQHVSSDKEVRAASTEADKRLSRFDIEMSMRGDIFERIVHLQETCDLGK IKPEARRYLEKSIKMGKRNGLHLPEQVQNEIKSMKKRMSELCIDFNKNLNEDDTFLVFSK AELGALPDDFIDSLEKTDDDKYKITLKYPHYFPVMKKCCIPETRRRMEMAFNTRCKEENT IILQQLLPLRTKVAKLLGYSTHADFVLEMNTAKSTSRVTAFLDDLSQKLKPLGEAEREFI LNLKKKECKDRGFEYDGKINAWDLYYYMTQTEELKYSIDQEFLKEYFPIEVVTEGLLNTY QELLGLSFEQMTDAHVWNKSVTLYTVKDKATGEVLGQFYLDLYPREGKYNHAACFGLQPG CLLPDGSRMMAVAALVVNFSQPVAGRPSLLRHDEVRTYFHEFGHVMHQICAQTDFARFSG TNVETDFVEVPSQMLENWVWDVDSLRRLSKHYKDGSPIADDLLEKLVASRLVNTGLLTLR QIVLSKVDQSLHTNTSLDAASEYAKYCSEILGVAATPGTNMPATFGHLAGGYDGQYYGYL WSEVFSMDMFYSCFKKEGIMNPEVGMKYRNLILKPGGSLDGMDMLHNFLKREPNQKAFLM SRGLHAP
>8VJU_2 Dynorphin A(1-13) (chains C) YGGFLRRIRPKLK
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
Water and common crystallization additives (EDO, CL, NA) are not listed.
Structural basis of divergent substrate recognition and inhibition of human neurolysin. Shi, K., Bagchi, S., Bickel, J. et al. Sci Rep (2024) 14:18420-18420. DOI 10.1038/s41598-024-67639-w · PubMed
Other PDB entries of the same protein (UniProt Q9BYT8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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