PDBsum entry 1qmy

Hydrolase

PDB id: 1qmy

Contents

Protein chains

156 a.a. *

Ligands

EDO ×2

Waters ×419

* Residue conservation analysis

PDB id:

1qmy

Name:

Hydrolase

Title:

Fmdv leader protease (lbshort-c51a-c133s)

Structure:

Protease. Chain: a, b, c. Synonym: leader protease. Engineered: yes. Mutation: yes

Source:

Aphthovirus o. Foot-and-mouth disease virus, fmdv. Organism_taxid: 12118. Strain: o1k. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.90Å R-factor: 0.190 R-free: 0.232

Authors:

A.Guarne,J.Tormo,W.Glaser,T.Skern,I.Fita

Date:

08-Oct-99 Release date: 12-Oct-00

Protein chains

P03305  (POLG_FMDVO) -  Genome polyprotein from Foot-and-mouth disease virus (isolate Bovine/Germany/O1Kaufbeuren/1966 serotype O)

Seq: 2332 a.a.

Struc: 156 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme reactions

• Enzyme class 1: E.C.2.7.7.48 - RNA-directed Rna polymerase.
• Reaction: RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate
• Enzyme class 2: E.C.3.4.22.28 - picornain 3C.
• Reaction: Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
• Enzyme class 3: E.C.3.4.22.46 - L-peptidase.
• Reaction: Autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly-|-Arg- and -Lys-|-Arg-.
• Enzyme class 4: E.C.3.6.1.15 - nucleoside-triphosphate phosphatase.
• Reaction: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + phosphate + H⁺

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site