PDB Information

PDB5JTQ
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/Protein Binding
Released2016-05-09
Resolution
CATH Insert Date19 Sep, 2016

PDB Images (11)

PDB Prints

PDB Chains (6)

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 Domchop allotted
F 20 Sep, 2016 Holding pen

CATH Domains (4)

Domain ID Date inserted into CATH Superfamily CATH Status
5jtqA00 06 Apr, 2017 3.10.420.10 Assigned
5jtqB00 16 Feb, 2017 3.10.420.10 Assigned
5jtqC00 16 Feb, 2017 3.10.420.10 Assigned
5jtqD00 16 Feb, 2017 3.10.420.10 Assigned

UniProtKB Entries (6)

Accession Gene ID Taxon Description
P0AG88 SECB_ECO57 Escherichia coli O157:H7 Protein-export protein SecB
P0AEY0 MALE_ECO57 Escherichia coli O157:H7 Maltose/maltodextrin-binding periplasmic protein
P0AG88 SECB_ECO57 Escherichia coli O157:H7 Protein-export protein SecB
P0AG88 SECB_ECO57 Escherichia coli O157:H7 Protein-export protein SecB
P0AEY0 MALE_ECO57 Escherichia coli O157:H7 Maltose/maltodextrin-binding periplasmic protein
P0AG88 SECB_ECO57 Escherichia coli O157:H7 Protein-export protein SecB