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

3F65

The F4 fimbrial chaperone FaeE does not self-cap its interactive surfaces

Functional Information from GO Data
ChainGOidnamespacecontents
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0043711biological_processpilus organization
A0071555biological_processcell wall organization
B0030288cellular_componentouter membrane-bounded periplasmic space
B0042597cellular_componentperiplasmic space
B0043711biological_processpilus organization
B0071555biological_processcell wall organization
C0030288cellular_componentouter membrane-bounded periplasmic space
C0042597cellular_componentperiplasmic space
C0043711biological_processpilus organization
C0071555biological_processcell wall organization
D0030288cellular_componentouter membrane-bounded periplasmic space
D0042597cellular_componentperiplasmic space
D0043711biological_processpilus organization
D0071555biological_processcell wall organization
E0030288cellular_componentouter membrane-bounded periplasmic space
E0042597cellular_componentperiplasmic space
E0043711biological_processpilus organization
E0071555biological_processcell wall organization
F0030288cellular_componentouter membrane-bounded periplasmic space
F0042597cellular_componentperiplasmic space
F0043711biological_processpilus organization
F0071555biological_processcell wall organization
G0030288cellular_componentouter membrane-bounded periplasmic space
G0042597cellular_componentperiplasmic space
G0043711biological_processpilus organization
G0071555biological_processcell wall organization
H0030288cellular_componentouter membrane-bounded periplasmic space
H0042597cellular_componentperiplasmic space
H0043711biological_processpilus organization
H0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD A 225
ChainResidue
AASP5
AGLN6
ATHR7
AARG8
AGLY195

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MPD C 225
ChainResidue
CILE146
CASP193
CHOH344
CGLU80
CPHE110
CARG112
CARG120

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD G 225
ChainResidue
GILE10
GGLU80
GPHE110
GARG112
GILE146
GLEU191

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 A 226
ChainResidue
AGLY126
ALYS204

Functional Information from PROSITE/UniProt
site_idPS00635
Number of Residues18
DetailsPILI_CHAPERONE Gram-negative pili assembly chaperone signature. LPkDKESVyWlNLqdIPP
ChainResidueDetails
ALEU75-PRO92

246031

PDB entries from 2025-12-10

PDB statisticsPDBj update infoContact PDBjnumon