PDB Information

PDB4ODM
MethodX-RAY DIFFRACTION
Host OrganismEscherichia coli
Gene SourceThermus thermophilus
Primary Citation
Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD.
Quistgaard, E.M., Weininger, U., Ural-Blimke, Y., Modig, K., Nordlund, P., Akke, M., Low, C.
BMC Biol.
HeaderIsomerase, Chaperone
Released2014-01-10
Resolution1.750
CATH Insert Date28 Jun, 2015

PDB Images (18)

PDB Prints

PDB Chains (13)

Chain ID Date inserted into CATH CATH Status
A 29 Jun, 2015 Chopped
B 29 Jun, 2015 Chopped
C 29 Jun, 2015 Chopped
D 29 Jun, 2015 Chopped
E 29 Jun, 2015 Rejected
F 29 Jun, 2015 Rejected
G 29 Jun, 2015 Rejected
H 29 Jun, 2015 Rejected
I 29 Jun, 2015 Rejected
J 29 Jun, 2015 Rejected
K 29 Jun, 2015 Rejected
L 29 Jun, 2015 Rejected
M 29 Jun, 2015 Rejected

CATH Domains (4)

Domain ID Date inserted into CATH Superfamily CATH Status
4odmA00 09 Jul, 2015 3.10.50.40 Assigned
4odmB00 10 Jul, 2015 3.10.50.40 Assigned
4odmC00 10 Jul, 2015 3.10.50.40 Assigned
4odmD00 10 Jul, 2015 3.10.50.40 Assigned

UniProtKB Entries (13)

Accession Gene ID Taxon Description
P0A7V0 RS2_ECOLI Escherichia coli K-12 30S ribosomal protein S2
P0A7V0 RS2_ECOLI Escherichia coli K-12 30S ribosomal protein S2
Q5SLE7 Q5SLE7_THET8 Thermus thermophilus HB8 Peptidyl-prolyl cis-trans isomerase
P0A7V0 RS2_ECOLI Escherichia coli K-12 30S ribosomal protein S2
P0A7V0 RS2_ECOLI Escherichia coli K-12 30S ribosomal protein S2
P0A7V0 RS2_ECOLI Escherichia coli K-12 30S ribosomal protein S2
Q5SLE7 Q5SLE7_THET8 Thermus thermophilus HB8 Peptidyl-prolyl cis-trans isomerase
P0A7V0 RS2_ECOLI Escherichia coli K-12 30S ribosomal protein S2
P0A7V0 RS2_ECOLI Escherichia coli K-12 30S ribosomal protein S2
P0A7V0 RS2_ECOLI Escherichia coli K-12 30S ribosomal protein S2
P0A7V0 RS2_ECOLI Escherichia coli K-12 30S ribosomal protein S2
Q5SLE7 Q5SLE7_THET8 Thermus thermophilus HB8 Peptidyl-prolyl cis-trans isomerase
Q5SLE7 Q5SLE7_THET8 Thermus thermophilus HB8 Peptidyl-prolyl cis-trans isomerase
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