1QMY: Fmdv leader protease

Fmdv leader protease (lbshort-C51A-C133S). Determined by X-ray diffraction at 1.9 Å resolution. Released 12 Oct 2000.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: APHTHOVIRUS O
Chains: 3
Atoms: 4,189
Mol. weight: 57.15 kDa
Released: 12 Oct 2000

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

Secondary structure: helices and β-sheets

1QMY contains 22 α-helices and 27 β-strands across 3 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: 7 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	30-32	3	1
β-strand	38-40	3	1
α-helix	51-63	13
α-helix	69-72	4
α-helix	79-90	12
α-helix	100-107	8
α-helix	108-110	3
β-strand	115-117	3	2
β-strand	124-126	3	2
α-helix	134-136	3
β-strand	137-144	8	2
β-strand	148-153	6	2
β-strand	160-163	4	2
β-strand	166-169	4	2
α-helix	174-176	3
β-strand	177-182	6	2

Chain B: 8 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	30-32	3	3
β-strand	38-40	3	3
α-helix	51-63	13
α-helix	66-68	3
α-helix	69-72	4
α-helix	79-90	12
α-helix	100-107	8
α-helix	108-110	3
β-strand	115-117	3	4
β-strand	124-126	3	4
α-helix	134-136	3
β-strand	137-144	8	4
β-strand	148-153	6	4
β-strand	160-163	4	4
β-strand	166-169	4	4
α-helix	174-176	3
β-strand	177-182	6	4

Chain C: 7 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	30-32	3	5
β-strand	38-40	3	5
α-helix	51-62	12
α-helix	69-72	4
α-helix	79-90	12
α-helix	100-107	8
α-helix	108-110	3
β-strand	115-117	3	6
β-strand	124-126	3	6
α-helix	134-136	3
β-strand	137-144	8	6
β-strand	148-153	6	6
β-strand	160-163	4	6
β-strand	166-169	4	6
α-helix	174-176	3
β-strand	177-182	6	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protease	A, B, C	protein	167	APHTHOVIRUS O	P03305

Sequence of entity 1 (A, B, C), FASTA

>1QMY_1 PROTEASE (chains A, B, C)
MELTLYNGEKKTFYSRPNNHDNAWLNAILQLFRYVEEPFFDWVYSSPENLTLEAIKQLED
LTGLELHEGGPPALVIWNIKHLLHTGIGTASRPSEVCVVDGTDMSLADFHAGIFLKGQEH
AVFACVTSNGWYAIDDEDFYPWTPDPSDVLVFVPYDQEPLNGEWKAK

Primary citation

Structure and Biochemical Features Distinguish the Foot-and-Mouth Disease Virus Leader Proteinase from Other Papain-Like Enzymes. Guarne, A., Hampoelz, B., Glaser, W. et al. J Mol Biol (2000) 302:1227. DOI 10.1006/JMBI.2000.4115 · PubMed

Other PDB entries of the same protein (UniProt P03305), best resolution first:

6FFA 1.5 Å, FMDV Leader protease bound to substrate ISG15
4QBB 1.6 Å, Structure of the foot-and-mouth disease virus leader proteinase in complex with…
9HV9 1.8 Å, Crystal structure of Fab34 complexed with a 7-mer peptide of FMDV VP1
1QQP 1.9 Å, Foot-and-mouth disease virus/ oligosaccharide receptor complex.
1QOL 3.0 Å, Structure of the fmdv leader protease
9HVA 3.89 Å, Crystal structure of Fab34 complexed with a 18-mer peptide of FMDV VP1
2JQF Full Length Leader Protease of Foot and Mouth Disease Virus C51A Mutant
2JQG Leader Protease

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