PDB Information

PDB5FCH
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
Resolution1.950
CATH Insert Date08 Jan, 2017

PDB Images (8)

PDB Prints

PDB Chains (3)

Chain ID Date inserted into CATH CATH Status
A 09 Jan, 2017 Chopped
B 09 Jan, 2017 Chopped
C 09 Jan, 2017 Rejected

CATH Domains (4)

Domain ID Date inserted into CATH Superfamily CATH Status
5fchA01 18 Jan, 2017 3.40.350.10 Assigned
5fchA02 18 Jan, 2017 3.90.230.10 Assigned
5fchB01 18 Jan, 2017 3.40.350.10 Assigned
5fchB02 18 Jan, 2017 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