PDB 3iaq

PDB Information

PDB3IAQ
MethodX-RAY DIFFRACTION
Host OrganismEscherichia coli
Gene SourceEscherichia coli K-12
Primary Citation
Studies of Glu-416 variants of beta-galactosidase (E. coli) show that the active site Mg(2+) is not important for structure and indicate that the main role of Mg (2+) is to mediate optimization of active site chemistry
Lo, S., Dugdale, M.L., Jeerh, N., Ku, T., Roth, N.J., Huber, R.E.
Protein J.
HeaderHydrolase
Released2009-07-14
Resolution2.700
CATH Insert Date31 Dec, 2009

PDB Images (25)

PDB Prints

PDB Chains (4)

Chain ID Date inserted into CATH CATH Status
A 31 Dec, 2009 Chopped
B 31 Dec, 2009 Chopped
C 31 Dec, 2009 Chopped
D 31 Dec, 2009 Chopped

CATH Domains (20)

Domain ID Date inserted into CATH Superfamily CATH Status
3iaqA01 16 Mar, 2010 2.60.120.260 Assigned
3iaqA02 16 Mar, 2010 2.60.40.10 Assigned
3iaqA03 16 Mar, 2010 3.20.20.80 Assigned
3iaqA04 16 Mar, 2010 2.60.40.10 Assigned
3iaqA05 16 Mar, 2010 2.70.98.10 Assigned
3iaqB01 16 Mar, 2010 2.60.120.260 Assigned
3iaqB02 16 Mar, 2010 2.60.40.10 Assigned
3iaqB03 16 Mar, 2010 3.20.20.80 Assigned
3iaqB04 16 Mar, 2010 2.60.40.10 Assigned
3iaqB05 16 Mar, 2010 2.70.98.10 Assigned
3iaqC01 16 Mar, 2010 2.60.120.260 Assigned
3iaqC02 16 Mar, 2010 2.60.40.10 Assigned
3iaqC03 16 Mar, 2010 3.20.20.80 Assigned
3iaqC04 16 Mar, 2010 2.60.40.10 Assigned
3iaqC05 16 Mar, 2010 2.70.98.10 Assigned
3iaqD01 16 Mar, 2010 2.60.120.260 Assigned
3iaqD02 16 Mar, 2010 2.60.40.10 Assigned
3iaqD03 16 Mar, 2010 3.20.20.80 Assigned
3iaqD04 16 Mar, 2010 2.60.40.10 Assigned
3iaqD05 16 Mar, 2010 2.70.98.10 Assigned

UniProtKB Entries (4)

Accession Gene ID Taxon Description
P00722 BGAL_ECOLI Escherichia coli K-12 Beta-galactosidase
P00722 BGAL_ECOLI Escherichia coli K-12 Beta-galactosidase
P00722 BGAL_ECOLI Escherichia coli K-12 Beta-galactosidase
P00722 BGAL_ECOLI Escherichia coli K-12 Beta-galactosidase