1LVM: Catalytically active tobacco etch virus protease

Catalytically active tobacco etch virus protease complexed with product. Determined by X-ray diffraction at 1.8 Å resolution. Released 27 Nov 2002.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Tobacco etch virus
Chains: 5
Atoms: 4,324
Mol. weight: 55.27 kDa
Released: 27 Nov 2002

Explore 1LVM in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1LVM contains 23 α-helices and 49 β-strands across 5 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: 11 helices, 23 β-strands

Element	Residues	Length	Sheet
α-helix	1-3	3
β-strand	5	1	1
α-helix	6	1
β-strand	9	1	2
α-helix	12-15	4
β-strand	18-25	8	3
β-strand	28-37	10	3
β-strand	40-43	4	3
α-helix	45-49	5
β-strand	54-59	6	3
β-strand	62-66	5	3
α-helix	69-71	3
β-strand	73-76	4	3
β-strand	83-86	4	3
α-helix	87-88	2
α-helix	92-94	3
β-strand	100	1	4
β-strand	108-111	4	4
β-strand	112-115	4	5
β-strand	122-125	4	5
β-strand	129-130	2	4
β-strand	132-134	3	4
β-strand	139-142	4	4
β-strand	144	1	6
α-helix	153	1
β-strand	154-157	4	4
β-strand	163-171	9	4
β-strand	177-181	5	4
α-helix	182-183	2
α-helix	186-191	6
α-helix	193-195	3
β-strand	198-200	3	3
β-strand	208-211	4	4
β-strand	214-217	4	4

Chain B: 10 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	6
β-strand	9	1	5
α-helix	12-15	4
β-strand	18-25	8	7
β-strand	28-37	10	7
β-strand	40-43	4	7
α-helix	45-48	4
β-strand	53-59	7	7
β-strand	62-66	5	7
α-helix	69-71	3
β-strand	73-76	4	7
β-strand	83-86	4	7
α-helix	87-88	2
α-helix	92-94	3
β-strand	100	1	8
β-strand	108-111	4	8
β-strand	112-114	3	2
α-helix	119-121	3
β-strand	123-125	3	2
β-strand	129-130	2	8
β-strand	132-134	3	8
β-strand	139-142	4	8
β-strand	144	1	1
α-helix	153	1
β-strand	154-157	4	8
β-strand	163-171	9	8
β-strand	177-181	5	8
α-helix	182-183	2
α-helix	186-191	6
α-helix	193-195	3
β-strand	198-200	3	7
β-strand	208-211	4	8
β-strand	214-217	4	8

Chains C and D: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	304-306	3	4

Chain E: 2 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	231	1
β-strand	232-233	2	3
α-helix	234	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Catalytic domain of the nuclear inclusion protein A (NIA)	A, B	protein	229	Tobacco etch virus	P04517
Oligopeptide substrate for the protease	C, D	protein	10	Tobacco etch virus	P04517
Catalytic domain of the nuclear inclusion protein A (NIA)	E	protein	7	Tobacco etch virus	P04517

Sequence of entity 1 (A, B), FASTA

>1LVM_1 CATALYTIC DOMAIN OF THE NUCLEAR INCLUSION PROTEIN A (NIA) (chains A, B)
GHHHHHHHGESLFKGPRDYNPISSTICHLTNESDGHTTSLYGIGFGPFIITNKHLFRRNN
GTLLVQSLHGVFKVKNTTTLQQHLIDGRDMIIIRMPKDFPPFPQKLKFREPQREERICLV
TTNFQTKSMSSMVSDTSCTFPSSDGIFWKHWIQTKDGQCGSPLVSTRDGFIVGIHSASNF
TNTNNYFTSVPKNFMELLTNQEAQQWVSGWRLNADSVLWGGHKVFMDKP

Sequence of entity 2 (C, D), FASTA

>1LVM_2 OLIGOPEPTIDE SUBSTRATE FOR THE PROTEASE (chains C, D)
XENLYFQSGT

Sequence of entity 3 (E), FASTA

>1LVM_3 CATALYTIC DOMAIN OF THE NUCLEAR INCLUSION PROTEIN A (NIA) (chains E)
EATQLMN

Primary citation

Structural basis for the substrate specificity of tobacco etch virus protease. Phan, J., Zdanov, A., Evdokimov, A.G. et al. J Biol Chem (2002) 277:50564-50572. DOI 10.1074/jbc.M207224200 · PubMed

Other PDB entries of the same protein (UniProt P04517), best resolution first:

1LVB 2.2 Å, Catalytically inactive tobacco etch virus protease complexed with substrate
1Q31 2.7 Å, Crystal Structure of the Tobacco Etch Virus Protease C151A mutant
9R9W 3.34 Å, RNA-free helical (h8.5) virus-like particle composed of TEV coat protein
6SUQ 3.7 Å, Crystal Structure of TcdB2-TccC3-TEV

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