1N0L

Crystal structure of the PapD chaperone (C-terminally 6x histidine-tagged) bound to the PapE pilus subunit (N-terminal-deleted) from uropathogenic E. coli

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0030288	cellular_component	outer membrane-bounded periplasmic space
A	0042597	cellular_component	periplasmic space
A	0043711	biological_process	pilus organization
A	0061077	biological_process	chaperone-mediated protein folding
A	0071555	biological_process	cell wall organization
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0007155	biological_process	cell adhesion
B	0009289	cellular_component	pilus
B	0043709	biological_process	cell adhesion involved in single-species biofilm formation
C	0005515	molecular_function	protein binding
C	0030288	cellular_component	outer membrane-bounded periplasmic space
C	0042597	cellular_component	periplasmic space
C	0043711	biological_process	pilus organization
C	0061077	biological_process	chaperone-mediated protein folding
C	0071555	biological_process	cell wall organization
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0007155	biological_process	cell adhesion
D	0009289	cellular_component	pilus
D	0043709	biological_process	cell adhesion involved in single-species biofilm formation

Functional Information from PROSITE/UniProt

site_id	PS00635
Number of Residues	18
Details	PILI_CHAPERONE Gram-negative pili assembly chaperone signature. LPqDRESLfYfNLreIPP

Chain	Residue	Details
A	LEU78-PRO95

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