PDB 3iap

PDB Information

PDB3IAP
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
Resolution2.000
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
3iapA01 16 Mar, 2010 2.60.120.260 Assigned
3iapA02 16 Mar, 2010 2.60.40.10 Assigned
3iapA03 16 Mar, 2010 3.20.20.80 Assigned
3iapA04 16 Mar, 2010 2.60.40.10 Assigned
3iapA05 16 Mar, 2010 2.70.98.10 Assigned
3iapB01 16 Mar, 2010 2.60.120.260 Assigned
3iapB02 16 Mar, 2010 2.60.40.10 Assigned
3iapB03 16 Mar, 2010 3.20.20.80 Assigned
3iapB04 16 Mar, 2010 2.60.40.10 Assigned
3iapB05 16 Mar, 2010 2.70.98.10 Assigned
3iapC01 16 Mar, 2010 2.60.120.260 Assigned
3iapC02 16 Mar, 2010 2.60.40.10 Assigned
3iapC03 16 Mar, 2010 3.20.20.80 Assigned
3iapC04 16 Mar, 2010 2.60.40.10 Assigned
3iapC05 16 Mar, 2010 2.70.98.10 Assigned
3iapD01 16 Mar, 2010 2.60.120.260 Assigned
3iapD02 16 Mar, 2010 2.60.40.10 Assigned
3iapD03 16 Mar, 2010 3.20.20.80 Assigned
3iapD04 16 Mar, 2010 2.60.40.10 Assigned
3iapD05 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