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6CD2

Crystal structure of the PapC usher bound to the chaperone-adhesin PapD-PapG

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0043711biological_processpilus organization
A0061077biological_processobsolete chaperone-mediated protein folding
A0071555biological_processcell wall organization
B0005576cellular_componentextracellular region
B0007155biological_processcell adhesion
B0009289cellular_componentpilus
B0030246molecular_functioncarbohydrate binding
C0009279cellular_componentcell outer membrane
C0009297biological_processpilus assembly
C0015473molecular_functionfimbrial usher porin activity
C0016020cellular_componentmembrane
C0042802molecular_functionidentical protein binding
C0055085biological_processtransmembrane transport
Functional Information from PROSITE/UniProt
site_idPS00635
Number of Residues18
DetailsPILI_CHAPERONE Gram-negative pili assembly chaperone signature. LPqDRESLfYfNLreIPP
ChainResidueDetails
ALEU78-PRO95

site_idPS01151
Number of Residues11
DetailsFIMBRIAL_USHER Fimbrial biogenesis outer membrane usher protein signature. VPAGPFsIQDL
ChainResidueDetails
CVAL288-LEU298

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PDB","id":"1J8R","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

245011

PDB entries from 2025-11-19

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