PDB 4p32

PDB Links
Overview

PDB Information

PDB	4P32
Method	X-RAY DIFFRACTION
Host Organism	Escherichia coli
Gene Source	Escherichia coli
Primary Citation	Decoupling catalytic activity from biological function of the ATPase that powers lipopolysaccharide transport. Sherman, D.J., Lazarus, M.B., Murphy, L., Liu, C., Walker, S., Ruiz, N., Kahne, D. Proc.Natl.Acad.Sci.USA
Header	Hydrolase
Released	2014-02-10
Resolution	1.550
CATH Insert Date	30 Mar, 2014

PDB Images (5)

Image of CATH 4p32

4p32

PDB 4p32

Image of CATH 4p32A

4p32A

PDB Chain 4p32A

Image of CATH 4p32B

4p32B

PDB Chain 4p32B

Image of CATH 4p32A00

4p32A00

CATH Domain 4p32A00

Image of CATH 4p32B00

4p32B00

CATH Domain 4p32B00

PDB Prints

PDB Chains (2)

Chain ID	Date inserted into CATH	CATH Status
A	31 Mar, 2014	Chopped
B	31 Mar, 2014	Chopped

CATH Domains (2)

Domain ID	Date inserted into CATH	Superfamily	CATH Status
4p32A00	25 Apr, 2014	3.40.50.300	Assigned
4p32B00	25 Apr, 2014	3.40.50.300	Assigned

UniProtKB Entries (2)

Accession	Gene ID	Taxon	Description
P0A9V1	LPTB_ECOLI	Escherichia coli K-12	Lipopolysaccharide export system ATP-binding protein LptB
P0A9V1	LPTB_ECOLI	Escherichia coli K-12	Lipopolysaccharide export system ATP-binding protein LptB