5LUZ: Human Neurolysin

Structure of Human Neurolysin (E475Q) in complex with neurotensin peptide products. Determined by X-ray diffraction at 2.7 Å resolution. Released 6 Dec 2017.

Method
X-ray diffraction
Resolution
2.7 Å
Organism
Homo sapiens
Chains
6
Atoms
10,950
Mol. weight
164.29 kDa
Ligands
ZN
Released
6 Dec 2017

Explore 5LUZ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5LUZ contains 81 α-helices and 30 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: 40 helices, 14 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-helix137-15216
α-helix159-18527
β-strand189-19241
β-strand21011
β-strand216-21941
α-helix222-23110
α-helix235-24511
α-helix250-27021
α-helix276-2816
α-helix289-32537
β-strand33412
α-helix335-35016
α-helix354-3574
α-helix358-3603
β-strand36213
α-helix363-37816
β-strand381-38554
β-strand396-40164
β-strand408-41584
β-strand427-43264
β-strand43615
β-strand44215
α-helix443-4442
β-strand445-45064
β-strand46313
α-helix466-48419
α-helix490-4923
α-helix504-5096
α-helix510-5134
α-helix516-5227
α-helix530-5334
α-helix534-5429
α-helix543-5453
α-helix548-56518
α-helix573-5808
α-helix581-5855
β-strand58812
α-helix589-5902
α-helix596-5983
α-helix600-6023
α-helix612-62312
α-helix624-6285
α-helix636-6427
α-helix643-6475
α-helix650-6523
α-helix655-6639
α-helix670-6767
Chain B: 41 helices, 14 β-strands
ElementResiduesLengthSheet
α-helix14-174
α-helix31-5424
α-helix62-665
α-helix67-8418
α-helix86-894
α-helix93-11422
α-helix117-12913
α-helix137-15216
α-helix159-18527
β-strand189-19246
α-helix202-2076
β-strand209-21026
β-strand216-21946
α-helix222-23110
α-helix235-24511
α-helix250-27021
α-helix276-2816
α-helix289-32537
β-strand33417
α-helix338-35013
α-helix354-3574
α-helix358-3603
β-strand36218
α-helix363-37816
β-strand381-38559
β-strand396-40169
β-strand408-41589
β-strand427-43269
β-strand436110
α-helix4411
β-strand442110
α-helix443-4442
β-strand445-45069
β-strand46318
α-helix466-48419
α-helix490-4923
α-helix504-5096
α-helix510-5134
α-helix516-5227
α-helix534-5429
α-helix543-5453
α-helix548-56518
α-helix573-5808
α-helix581-5855
β-strand58817
α-helix589-5902
α-helix595-5984
α-helix600-6023
α-helix612-62312
α-helix624-6285
α-helix636-6427
α-helix643-6475
α-helix650-6523
α-helix655-6639
α-helix670-6767
Chain C: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand914
Chain D: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand819

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Neurolysin, mitochondrialA, Bprotein686Homo sapiensQ9BYT8 (AlphaFold model)
PRO-ARG-ARG-PRO neurotensin fragmentC, D, P, Qprotein13Homo sapiensP30990 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>5LUZ_1 Neurolysin, mitochondrial (chains A, B)
MGSSHHHHHHSSGLVPRGSSSYTVAGRNVLRWDLSPEQIKTRTEELIVQTKQVYDAVGML
GIEEVTYENCLQALADVEVKYIVERTMLDFPQHVSSDKEVRAASTEADKRLSRFDIEMSM
RGDIFERIVHLQETCDLGKIKPEARRYLEKSIKMGKRNGLHLPEQVQNEIKSMKKRMSEL
CIDFNKNLNEDDTFLVFSKAELGALPDDFIDSLEKTDDDKYKITLKYPHYFPVMKKCCIP
ETRRRMEMAFNTRCKEENTIILQQLLPLRTKVAKLLGYSTHADFVLEMNTAKSTSRVTAF
LDDLSQKLKPLGEAEREFILNLKKKECKDRGFEYDGKINAWDLYYYMTQTEELKYSIDQE
FLKEYFPIEVVTEGLLNTYQELLGLSFEQMTDAHVWNKSVTLYTVKDKATGEVLGQFYLD
LYPREGKYNHAACFGLQPGCLLPDGSRMMAVAALVVNFSQPVAGRPSLLRHDEVRTYFHQ
FGHVMHQICAQTDFARFSGTNVETDFVEVPSQMLENWVWDVDSLRRLSKHYKDGSPIADD
LLEKLVASRLVNTGLLTLRQIVLSKVDQSLHTNTSLDAASEYAKYCSEILGVAATPGTNM
PATFGHLAGGYDGQYYGYLWSEVFSMDMFYSCFKKEGIMNPEVGMKYRNLILKPGGSLDG
MDMLHNFLKREPNQKAFLMSRGLHAP
Sequence of entity 2 (C, D, P, Q), FASTA
>5LUZ_2 PRO-ARG-ARG-PRO neurotensin fragment (chains C, D, P, Q)
QLYENKPRRPYIL

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2

Water and common crystallization additives (GOL, CL) are not listed.

Primary citation

Mechanism of Peptide Binding and Cleavage by the Human Mitochondrial Peptidase Neurolysin. Teixeira, P.F., Masuyer, G., Pinho, C.M. et al. J Mol Biol (2018) 430:348-362. DOI 10.1016/j.jmb.2017.11.011 · 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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