PDB Information

PDB5FCF
MethodX-RAY DIFFRACTION
Host OrganismEscherichia coli BL21(DE3)
Gene SourceXanthomonas campestris pv. campestris str. ATCC 33913
Primary Citation
Crystal structure and biochemical investigations reveal novel mode of substrate selectivity and illuminate substrate inhibition and allostericity in a subfamily of Xaa-Pro dipeptidases.
Are, V.N., Kumar, A., Kumar, S., Goyal, V.D., Ghosh, B., Bhatnagar, D., Jamdar, S.N., Makde, R.D.
Biochim. Biophys. Acta
HeaderHydrolase
Released2015-12-15
Resolution1.850
CATH Insert Date25 Dec, 2016

PDB Images (8)

PDB Prints

PDB Chains (3)

Chain ID Date inserted into CATH CATH Status
A 26 Dec, 2016 Chopped
B 26 Dec, 2016 Chopped
C 26 Dec, 2016 Rejected

CATH Domains (4)

Domain ID Date inserted into CATH Superfamily CATH Status
5fcfA01 29 Dec, 2016 3.40.350.10 Assigned
5fcfA02 29 Dec, 2016 3.90.230.10 Assigned
5fcfB01 29 Dec, 2016 3.40.350.10 Assigned
5fcfB02 29 Dec, 2016 3.90.230.10 Assigned

UniProtKB Entries (2)

Accession Gene ID Taxon Description
Q8P839 Q8P839_XANCP Xanthomonas campestris pv. campestris str. ATCC 33913 Proline dipeptidase
Q8P839 Q8P839_XANCP Xanthomonas campestris pv. campestris str. ATCC 33913 Proline dipeptidase