8VJW: Human Neurolysin

Structure of Human Neurolysin in complex with angiotensin I peptide. Determined by X-ray diffraction at 2.49 Å resolution. Released 21 Aug 2024.

Method
X-ray diffraction
Resolution
2.49 Å
Organism
Homo sapiens
Chains
6
Atoms
10,838
Mol. weight
155.99 kDa
Ligands
ZN
Released
21 Aug 2024

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

Secondary structure: helices and β-sheets

8VJW contains 89 α-helices and 26 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.

Chain A: 45 helices, 13 β-strands

ElementResiduesLengthSheet
α-helix31-5323
α-helix62-665
α-helix67-8418
α-helix86-883
α-helix93-11422
α-helix117-12913
α-helix132-1343
α-helix137-15115
α-helix159-18426
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-helix289-30214
α-helix304-32522
α-helix335-3373
α-helix338-35013
α-helix354-3574
α-helix358-3603
β-strand36212
α-helix363-37715
β-strand380-38453
α-helix3851
β-strand396-40273
β-strand408-41583
β-strand427-42823
β-strand43213
β-strand43614
β-strand44214
α-helix443-4442
β-strand445-45063
α-helix453-4564
α-helix461-4622
β-strand46312
α-helix466-48419
α-helix490-4923
α-helix503-5086
α-helix509-5135
α-helix516-5227
α-helix534-5429
α-helix548-56518
α-helix573-5808
α-helix581-5855
α-helix588-5903
α-helix596-5983
α-helix600-6034
α-helix612-62312
α-helix624-6285
α-helix629-6313
α-helix636-6427
α-helix643-6475
α-helix655-6639
α-helix670-6745
Chain B: 44 helices, 13 β-strands
ElementResiduesLengthSheet
α-helix31-5323
α-helix62-665
α-helix67-8418
α-helix86-883
α-helix93-11422
α-helix117-12913
α-helix132-1343
α-helix137-15115
α-helix159-18426
β-strand189-19245
α-helix195-1973
α-helix202-2054
β-strand21015
β-strand216-21945
α-helix222-23110
α-helix235-24511
α-helix250-27021
α-helix276-2816
α-helix289-30214
α-helix304-32522
α-helix335-3373
α-helix338-35013
α-helix354-3574
α-helix358-3603
β-strand36216
α-helix363-37715
β-strand380-38567
β-strand395-40287
β-strand408-41587
β-strand427-42827
β-strand43217
β-strand43618
β-strand44218
α-helix443-4442
β-strand445-45067
α-helix454-4563
α-helix461-4622
β-strand46316
α-helix466-48419
α-helix490-4923
α-helix503-5086
α-helix509-5135
α-helix516-5227
α-helix534-5429
α-helix548-56518
α-helix573-5808
α-helix581-5855
α-helix588-5903
α-helix596-5983
α-helix600-6034
α-helix612-62312
α-helix624-6285
α-helix629-6313
α-helix636-6427
α-helix643-6475
α-helix655-6639
α-helix670-6745

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Neurolysin, mitochondrialA, Bprotein667Homo sapiensQ9BYT8 (AlphaFold model)
Angiotensin-1 peptide N-terminal endC, Eprotein4Homo sapiens
Angiotensin-1 peptide C-terminal endD, Fprotein6Homo sapiens
Sequence of entity 1 (A, B), FASTA
>8VJW_1 Neurolysin, mitochondrial (chains A, B)
SSYTVAGRNVLRWDLSPEQIKTRTEELIVQTKQVYDAVGMLGIEEVTYENCLQALADVEV
KYIVERTMLDFPQHVSSDKEVRAASTEADKRLSRFDIEMSMRGDIFERIVHLQETCDLGK
IKPEARRYLEKSIKMGKRNGLHLPEQVQNEIKSMKKRMSELCIDFNKNLNEDDTFLVFSK
AELGALPDDFIDSLEKTDDDKYKITLKYPHYFPVMKKCCIPETRRRMEMAFNTRCKEENT
IILQQLLPLRTKVAKLLGYSTHADFVLEMNTAKSTSRVTAFLDDLSQKLKPLGEAEREFI
LNLKKKECKDRGFEYDGKINAWDLYYYMTQTEELKYSIDQEFLKEYFPIEVVTEGLLNTY
QELLGLSFEQMTDAHVWNKSVTLYTVKDKATGEVLGQFYLDLYPREGKYNHAACFGLQPG
CLLPDGSRMMAVAALVVNFSQPVAGRPSLLRHDEVRTYFHEFGHVMHQICAQTDFARFSG
TNVETDFVEVPSQMLENWVWDVDSLRRLSKHYKDGSPIADDLLEKLVASRLVNTGLLTLR
QIVLSKVDQSLHTNTSLDAASEYAKYCSEILGVAATPGTNMPATFGHLAGGYDGQYYGYL
WSEVFSMDMFYSCFKKEGIMNPEVGMKYRNLILKPGGSLDGMDMLHNFLKREPNQKAFLM
SRGLHAP
Sequence of entity 2 (C, E), FASTA
>8VJW_2 Angiotensin-1 peptide N-terminal end (chains C, E)
DRVY
Sequence of entity 3 (D, F), FASTA
>8VJW_3 Angiotensin-1 peptide C-terminal end (chains D, F)
IHPFHL

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2

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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