PDB Information

PDB1ECQ
MethodX-RAY DIFFRACTION
Host OrganismEscherichia coli
Gene SourceEscherichia coli
Primary Citation
Evolution of enzymatic activities in the enolase superfamily: crystallographic and mutagenesis studies of the reaction catalyzed by D-glucarate dehydratase from Escherichia coli.
Gulick, A.M., Hubbard, B.K., Gerlt, J.A., Rayment, I.
Biochemistry
HeaderLyase
Released2000-01-25
Resolution2.000
CATH Insert Date05 Mar, 2006

PDB Images (13)

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 (8)

Domain ID Date inserted into CATH Superfamily CATH Status
1ecqA01 05 Mar, 2006 3.30.390.10 Assigned
1ecqA02 05 Mar, 2006 3.20.20.120 Assigned
1ecqB01 05 Mar, 2006 3.30.390.10 Assigned
1ecqB02 05 Mar, 2006 3.20.20.120 Assigned
1ecqC01 05 Mar, 2006 3.30.390.10 Assigned
1ecqC02 05 Mar, 2006 3.20.20.120 Assigned
1ecqD01 05 Mar, 2006 3.30.390.10 Assigned
1ecqD02 05 Mar, 2006 3.20.20.120 Assigned

UniProtKB Entries (4)

Accession Gene ID Taxon Description
P0AES2 GUDD_ECOLI Escherichia coli K-12 Glucarate dehydratase
P0AES2 GUDD_ECOLI Escherichia coli K-12 Glucarate dehydratase
P0AES2 GUDD_ECOLI Escherichia coli K-12 Glucarate dehydratase
P0AES2 GUDD_ECOLI Escherichia coli K-12 Glucarate dehydratase