PDB Information

PDB5JTO
MethodSOLUTION NMR
Host OrganismEscherichia coli BL21(DE3)
Gene SourceEscherichia coli O157:H7
Primary Citation
Structural basis for the antifolding activity of a molecular chaperone.
Huang, C., Rossi, P., Saio, T., Kalodimos, C.G.
Nature
HeaderChaperone/Hydrolase
Released2016-05-09
Resolution
CATH Insert Date19 Sep, 2016

PDB Images (13)

PDB Prints

PDB Chains (8)

Chain ID Date inserted into CATH CATH Status
A 20 Sep, 2016 Chopped
B 20 Sep, 2016 Chopped
C 20 Sep, 2016 Chopped
D 20 Sep, 2016 Chopped
E 20 Sep, 2016 Holding pen
F 20 Sep, 2016 Holding pen
G 20 Sep, 2016 Domchop allotted
H 20 Sep, 2016 Holding pen

CATH Domains (4)

Domain ID Date inserted into CATH Superfamily CATH Status
5jtoA00 06 Apr, 2017 3.10.420.10 Assigned
5jtoB00 16 Feb, 2017 3.10.420.10 Assigned
5jtoC00 06 Apr, 2017 3.10.420.10 Assigned
5jtoD00 06 Apr, 2017 3.10.420.10 Assigned

UniProtKB Entries (8)

Accession Gene ID Taxon Description
P0AG88 SECB_ECO57 Escherichia coli O157:H7 Protein-export protein SecB
P00634 PPB_ECOLI Escherichia coli K-12 Alkaline phosphatase
P00634 PPB_ECOLI Escherichia coli K-12 Alkaline phosphatase
P0AG88 SECB_ECO57 Escherichia coli O157:H7 Protein-export protein SecB
P00634 PPB_ECOLI Escherichia coli K-12 Alkaline phosphatase
P0AG88 SECB_ECO57 Escherichia coli O157:H7 Protein-export protein SecB
P0AG88 SECB_ECO57 Escherichia coli O157:H7 Protein-export protein SecB
P00634 PPB_ECOLI Escherichia coli K-12 Alkaline phosphatase