1LVB: PDB entry 1LVB

Catalytically inactive tobacco etch virus protease complexed with substrate. Determined by X-ray diffraction at 2.2 Å resolution. Released 27 Nov 2002.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Tobacco etch virus
Chains: 4
Atoms: 3,783
Mol. weight: 58.51 kDa
Released: 27 Nov 2002

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

Secondary structure: helices and β-sheets

1LVB contains 17 α-helices and 43 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: 9 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	12-15	4
β-strand	18-25	8	1
β-strand	28-37	10	1
β-strand	40-43	4	1
α-helix	45-48	4
β-strand	53-59	7	1
β-strand	62-66	5	1
α-helix	69-71	3
β-strand	73-76	4	1
α-helix	77	1
β-strand	83-86	4	1
α-helix	92-94	3
β-strand	100	1	2
β-strand	109-111	3	2
β-strand	112-116	5	3
β-strand	120-125	6	3
α-helix	126-128	3
β-strand	129	1	2
β-strand	132-134	3	2
β-strand	139-142	4	2
β-strand	154-157	4	2
β-strand	163-171	9	2
β-strand	177-181	5	2
α-helix	182-183	2
α-helix	186-191	6
α-helix	193-195	3
β-strand	199	1	1
β-strand	208-211	4	2
β-strand	214-217	4	2

Chain B: 8 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	12-15	4
β-strand	18-25	8	4
β-strand	28-37	10	4
β-strand	40-43	4	4
α-helix	45-48	4
β-strand	53-59	7	4
β-strand	62-66	5	4
α-helix	69-71	3
β-strand	73-76	4	4
α-helix	77	1
β-strand	83-86	4	4
α-helix	92-94	3
β-strand	100	1	5
β-strand	108-111	4	5
β-strand	112-116	5	3
β-strand	120-125	6	3
β-strand	129-133	5	5
β-strand	139-142	4	5
β-strand	154-157	4	5
β-strand	163-171	9	5
β-strand	177-181	5	5
α-helix	182-183	2
α-helix	186-191	6
α-helix	193-195	3
β-strand	199	1	4
β-strand	208-211	4	5
β-strand	214-217	4	5

Chains C and D: 0 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	304-306	3	2
β-strand	309	1	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Catalytic domain of the nuclear inclusion protein A (NIA)	A, B	protein	243	Tobacco etch virus	P04517
Oligopeptide substrate for the protease	C, D	protein	10		P04517

Sequence of entity 1 (A, B), FASTA

>1LVB_1 CATALYTIC DOMAIN OF THE NUCLEAR INCLUSION PROTEIN A (NIA) (chains A, B)
SHHHHHHGESLFKGPRDYNPISSTICHLTNESDGHTTSLYGIGFGPFIITNKHLFRRNNG
TLLVQSLHGVFKVKNTTTLQQHLIDGRDMIIIRMPKDFPPFPQKLKFREPQREERICLVT
TNFQTKSMSSMVSDTSCTFPSSDGIFWKHWIQTKDGQAGSPLVSTRDGFIVGIHSASNFT
NTNNYFTSVPKNFMELLTNQEAQQWVSGWRLNADSVLWGGHKVFMSKPEEPFQPVKEATQ
LMN

Sequence of entity 2 (C, D), FASTA

>1LVB_2 OLIGOPEPTIDE SUBSTRATE FOR THE PROTEASE (chains C, D)
TENLYFQSGT

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:

1LVM 1.8 Å, Catalytically active tobacco etch virus protease complexed with product
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

Browse structure collections

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