6SWH

Crystal structure of the ternary complex between the type 1 pilus proteins FimC, FimI and FimA from E. coli

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0006457	biological_process	protein folding
A	0030288	cellular_component	outer membrane-bounded periplasmic space
A	0042597	cellular_component	periplasmic space
A	0043711	biological_process	pilus organization
A	0044183	molecular_function	protein folding chaperone
A	0061077	biological_process	obsolete chaperone-mediated protein folding
A	0071555	biological_process	cell wall organization
B	0007155	biological_process	cell adhesion
B	0009289	cellular_component	pilus
B	0009297	biological_process	pilus assembly
B	0043709	biological_process	cell adhesion involved in single-species biofilm formation
C	0007155	biological_process	cell adhesion
C	0009289	cellular_component	pilus
C	0042802	molecular_function	identical protein binding
C	0043709	biological_process	cell adhesion involved in single-species biofilm formation
D	0005515	molecular_function	protein binding
D	0006457	biological_process	protein folding
D	0030288	cellular_component	outer membrane-bounded periplasmic space
D	0042597	cellular_component	periplasmic space
D	0043711	biological_process	pilus organization
D	0044183	molecular_function	protein folding chaperone
D	0061077	biological_process	obsolete chaperone-mediated protein folding
D	0071555	biological_process	cell wall organization
E	0007155	biological_process	cell adhesion
E	0009289	cellular_component	pilus
E	0009297	biological_process	pilus assembly
E	0043709	biological_process	cell adhesion involved in single-species biofilm formation
F	0007155	biological_process	cell adhesion
F	0009289	cellular_component	pilus
F	0042802	molecular_function	identical protein binding
F	0043709	biological_process	cell adhesion involved in single-species biofilm formation

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue PEG A 301

Chain	Residue
A	PRO124
A	TYR149
A	LEU150
A	ILE190
A	ASN191
A	ASP192

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site_id	AC2
Number of Residues	4
Details	binding site for residue EDO B 201

Chain	Residue
B	GLN160
B	GLY73
B	PRO118
B	ASN120

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU75-SER92

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