Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4AY0

High resolution crystal structure of the monomeric subunit-free Caf1M chaperone

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0006457biological_processprotein folding
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0043711biological_processpilus organization
A0044183molecular_functionprotein folding chaperone
A0061077biological_processobsolete chaperone-mediated protein folding
A0071555biological_processcell wall organization
B0005515molecular_functionprotein binding
B0006457biological_processprotein folding
B0030288cellular_componentouter membrane-bounded periplasmic space
B0042597cellular_componentperiplasmic space
B0043711biological_processpilus organization
B0044183molecular_functionprotein folding chaperone
B0061077biological_processobsolete chaperone-mediated protein folding
B0071555biological_processcell wall organization
Functional Information from PROSITE/UniProt
site_idPS00635
Number of Residues18
DetailsPILI_CHAPERONE Gram-negative pili assembly chaperone signature. FPrDKESLkWlCVkgIPP
ChainResidueDetails
APHE87-PRO104

238268

PDB entries from 2025-07-02

PDB statisticsPDBj update infoContact PDBjnumon