PDB Information

PDB1YDN
MethodX-RAY DIFFRACTION
Host OrganismEscherichia coli
Gene SourceBrucella melitensis
Primary Citation
Crystal structures of two bacterial 3-hydroxy-3-methylglutaryl-CoA lyases suggest a common catalytic mechanism among a family of TIM barrel metalloenzymes cleaving carbon-carbon bonds.
Forouhar, F., Hussain, M., Farid, R., Benach, J., Abashidze, M., Edstrom, W.C., Vorobiev, S.M., Xiao, R., Acton, T.B., Fu, Z., Kim, J.J., Miziorko, H.M., Montelione, G.T., Hunt, J.F.
J.Biol.Chem.
HeaderLyase
Released2004-12-24
Resolution2.300
CATH Insert Date05 Mar, 2006

PDB Images (9)

PDB Prints

PDB Chains (4)

Chain ID Date inserted into CATH CATH Status
A 05 Mar, 2006 Chopped
B 05 Mar, 2006 Chopped
C 05 Mar, 2006 Chopped
D 05 Mar, 2006 Chopped

CATH Domains (4)

Domain ID Date inserted into CATH Superfamily CATH Status
1ydnA00 26 Oct, 2009 3.20.20.70 Assigned
1ydnB00 09 Jul, 2007 3.20.20.70 Assigned
1ydnC00 26 Oct, 2009 3.20.20.70 Assigned
1ydnD00 09 Jul, 2007 3.20.20.70 Assigned

UniProtKB Entries (4)

Accession Gene ID Taxon Description
Q8YEF2 Q8YEF2_BRUME Brucella melitensis bv. 1 str. 16M Hydroxymethylglutaryl-CoA lyase
Q8YEF2 Q8YEF2_BRUME Brucella melitensis bv. 1 str. 16M Hydroxymethylglutaryl-CoA lyase
Q8YEF2 Q8YEF2_BRUME Brucella melitensis bv. 1 str. 16M Hydroxymethylglutaryl-CoA lyase
Q8YEF2 Q8YEF2_BRUME Brucella melitensis bv. 1 str. 16M Hydroxymethylglutaryl-CoA lyase