8VJY: Human Neurolysin

Structure of Human Neurolysin in complex with Neurotensin peptide. Determined by X-ray diffraction at 1.95 Å resolution. Released 21 Aug 2024.

Method
X-ray diffraction
Resolution
1.95 Å
Organism
Homo sapiens
Chains
4
Atoms
12,083
Mol. weight
158.45 kDa
Ligands
ZN
Released
21 Aug 2024

Explore 8VJY in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8VJY contains 92 α-helices and 28 β-strands across 4 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.

Chain A: 47 helices, 14 β-strands

ElementResiduesLengthSheet
α-helix31-5424
α-helix57-593
α-helix62-676
α-helix68-8417
α-helix86-894
α-helix93-11422
α-helix117-12913
α-helix132-1343
α-helix137-15115
α-helix159-18527
β-strand189-19241
α-helix195-1973
α-helix202-2054
β-strand209-21021
β-strand216-21941
α-helix222-23110
α-helix235-24511
α-helix250-27021
α-helix276-2816
α-helix289-32537
α-helix335-3373
α-helix338-35013
α-helix354-3574
α-helix358-3603
β-strand36212
α-helix363-37816
β-strand380-38453
α-helix3851
β-strand396-40273
β-strand408-41583
β-strand427-43263
β-strand43514
β-strand43615
α-helix4411
β-strand44215
α-helix443-4442
β-strand445-45063
α-helix453-4564
β-strand46312
α-helix466-48419
β-strand48714
α-helix490-4923
α-helix504-5107
α-helix511-5133
α-helix516-5216
α-helix530-5334
α-helix534-5429
α-helix543-5453
α-helix548-56518
α-helix573-5808
α-helix581-5855
α-helix588-5903
α-helix595-5984
α-helix600-6034
α-helix612-62312
α-helix624-6296
α-helix630-6312
α-helix636-6427
α-helix643-6475
α-helix655-6639
α-helix670-6767
Chains B and D: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand813
Chain C: 45 helices, 12 β-strands
ElementResiduesLengthSheet
α-helix31-5424
α-helix62-665
α-helix67-8418
α-helix86-894
α-helix93-11422
α-helix117-12913
α-helix132-1343
α-helix137-15115
α-helix159-18527
β-strand189-19246
α-helix195-1973
α-helix202-2054
β-strand209-21026
β-strand216-21946
α-helix222-23110
α-helix235-24511
α-helix250-27021
α-helix276-2816
α-helix289-32537
α-helix335-3373
α-helix338-35013
α-helix354-3574
α-helix358-3603
β-strand36217
α-helix363-37816
β-strand380-38568
β-strand396-40278
β-strand408-41588
β-strand427-43268
β-strand43619
α-helix4411
β-strand44219
α-helix443-4442
β-strand445-45068
α-helix453-4564
β-strand46317
α-helix466-48419
α-helix490-4923
α-helix504-5107
α-helix511-5133
α-helix516-5216
α-helix530-5334
α-helix534-5429
α-helix543-5453
α-helix548-56518
α-helix573-5808
α-helix581-5855
α-helix588-5903
α-helix595-5984
α-helix600-6034
α-helix612-62312
α-helix624-6296
α-helix630-6312
α-helix636-6427
α-helix643-6475
α-helix655-6639
α-helix670-6756

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Neurolysin, mitochondrialA, Cprotein667Homo sapiensQ9BYT8 (AlphaFold model)
NeurotensinB, Dprotein14Homo sapiensP30990 (AlphaFold model)
Sequence of entity 1 (A, C), FASTA
>8VJY_1 Neurolysin, mitochondrial (chains A, C)
SSYTVAGRNVLRWDLSPEQIKTRTEELIVQTKQVYDAVGMLGIEEVTYENCLQALADVEV
KYIVERTMLDFPQHVSSDKEVRAASTEADKRLSRFDIEMSMRGDIFERIVHLQETCDLGK
IKPEARRYLEKSIKMGKRNGLHLPEQVQNEIKSMKKRMSELCIDFNKNLNEDDTFLVFSK
AELGALPDDFIDSLEKTDDDKYKITLKYPHYFPVMKKCCIPETRRRMEMAFNTRCKEENT
IILQQLLPLRTKVAKLLGYSTHADFVLEMNTAKSTSRVTAFLDDLSQKLKPLGEAEREFI
LNLKKKECKDRGFEYDGKINAWDLYYYMTQTEELKYSIDQEFLKEYFPIEVVTEGLLNTY
QELLGLSFEQMTDAHVWNKSVTLYTVKDKATGEVLGQFYLDLYPREGKYNHAACFGLQPG
CLLPDGSRMMAVAALVVNFSQPVAGRPSLLRHDEVRTYFHEFGHVMHQICAQTDFARFSG
TNVETDFVEVPSQMLENWVWDVDSLRRLSKHYKDGSPIADDLLEKLVASRLVNTGLLTLR
QIVLSKVDQSLHTNTSLDAASEYAKYCSEILGVAATPGTNMPATFGHLAGGYDGQYYGYL
WSEVFSMDMFYSCFKKEGIMNPEVGMKYRNLILKPGGSLDGMDMLHNFLKREPNQKAFLM
SRGLHAP
Sequence of entity 2 (B, D), FASTA
>8VJY_2 Neurotensin (chains B, D)
PQLYENKPRRPYIL

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2

Water and common crystallization additives (EDO) are not listed.

Primary citation

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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