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4DJM

Crystal structure of the E. coli chaperone DraB

Functional Information from GO Data
ChainGOidnamespacecontents
A0030288cellular_componentouter membrane-bounded periplasmic space
A0043711biological_processpilus organization
A0071555biological_processcell wall organization
B0030288cellular_componentouter membrane-bounded periplasmic space
B0043711biological_processpilus organization
B0071555biological_processcell wall organization
C0030288cellular_componentouter membrane-bounded periplasmic space
C0043711biological_processpilus organization
C0071555biological_processcell wall organization
D0030288cellular_componentouter membrane-bounded periplasmic space
D0043711biological_processpilus organization
D0071555biological_processcell wall organization
E0030288cellular_componentouter membrane-bounded periplasmic space
E0043711biological_processpilus organization
E0071555biological_processcell wall organization
F0030288cellular_componentouter membrane-bounded periplasmic space
F0043711biological_processpilus organization
F0071555biological_processcell wall organization
G0030288cellular_componentouter membrane-bounded periplasmic space
G0043711biological_processpilus organization
G0071555biological_processcell wall organization
H0030288cellular_componentouter membrane-bounded periplasmic space
H0043711biological_processpilus organization
H0071555biological_processcell wall organization
Functional Information from PROSITE/UniProt
site_idPS00635
Number of Residues18
DetailsPILI_CHAPERONE Gram-negative pili assembly chaperone signature. FPpDRESLqWiCVkgIPP
ChainResidueDetails
APHE95-PRO112

246704

PDB entries from 2025-12-24

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