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7LHH

Cryo-EM structure of E. coli P pilus tip assembly intermediate PapC-PapD-PapK-PapG in the second conformation

Functional Information from GO Data
ChainGOidnamespacecontents
C0009279cellular_componentcell outer membrane
C0009297biological_processpilus assembly
C0015473molecular_functionfimbrial usher porin activity
C0016020cellular_componentmembrane
C0042802molecular_functionidentical protein binding
C0055085biological_processtransmembrane transport
D0005515molecular_functionprotein binding
D0030288cellular_componentouter membrane-bounded periplasmic space
D0042597cellular_componentperiplasmic space
D0043711biological_processpilus organization
D0061077biological_processchaperone-mediated protein folding
D0071555biological_processcell wall organization
G0007155biological_processcell adhesion
G0009289cellular_componentpilus
G0030246molecular_functioncarbohydrate binding
K0007155biological_processcell adhesion
K0009289cellular_componentpilus
Functional Information from PROSITE/UniProt
site_idPS00635
Number of Residues18
DetailsPILI_CHAPERONE Gram-negative pili assembly chaperone signature. LPqDRESLfYfNLreIPP
ChainResidueDetails
DLEU78-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 Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:1J8R
ChainResidueDetails
GGLU79
GGLY124

219869

PDB entries from 2024-05-15

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