PDB Information

PDB2O1C
MethodX-RAY DIFFRACTION
Host OrganismEscherichia coli
Gene SourceEscherichia coli
Primary Citation
Structure and function of the E. coli dihydroneopterin triphosphate pyrophosphatase: a Nudix enzyme involved in folate biosynthesis.
Gabelli, S.B., Bianchet, M.A., Xu, W., Dunn, C.A., Niu, Z.D., Amzel, L.M., Bessman, M.J.
Structure
HeaderHydrolase
Released2006-11-28
Resolution1.800
CATH Insert Date07 Nov, 2007

PDB Images (9)

PDB Prints

PDB Chains (4)

Chain ID Date inserted into CATH CATH Status
A 08 Nov, 2007 Chopped
B 08 Nov, 2007 Chopped
C 08 Nov, 2007 Chopped
D 08 Nov, 2007 Chopped

CATH Domains (4)

Domain ID Date inserted into CATH Superfamily CATH Status
2o1cA00 18 Mar, 2013 3.90.79.10 Assigned
2o1cB00 18 Mar, 2013 3.90.79.10 Assigned
2o1cC00 18 Mar, 2013 3.90.79.10 Assigned
2o1cD00 18 Mar, 2013 3.90.79.10 Assigned

UniProtKB Entries (4)

Accession Gene ID Taxon Description
P0AFC0 NUDB_ECOLI Escherichia coli K-12 Dihydroneopterin triphosphate diphosphatase
P0AFC0 NUDB_ECOLI Escherichia coli K-12 Dihydroneopterin triphosphate diphosphatase
P0AFC0 NUDB_ECOLI Escherichia coli K-12 Dihydroneopterin triphosphate diphosphatase
P0AFC0 NUDB_ECOLI Escherichia coli K-12 Dihydroneopterin triphosphate diphosphatase