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3BWU

Crystal structure of the ternary complex of FimD (N-Terminal Domain, FimDN) with FimC and the N-terminally truncated pilus subunit FimF (FimFt)

Functional Information from GO Data
ChainGOidnamespacecontents
C0005515molecular_functionprotein binding
C0030288cellular_componentouter membrane-bounded periplasmic space
C0042597cellular_componentperiplasmic space
C0043711biological_processpilus organization
C0044183molecular_functionprotein folding chaperone
C0061077biological_processchaperone-mediated protein folding
C0071555biological_processcell wall organization
D0009297biological_processpilus assembly
D0015473molecular_functionfimbrial usher porin activity
D0016020cellular_componentmembrane
F0007155biological_processcell adhesion
F0007638biological_processmechanosensory behavior
F0009289cellular_componentpilus
F0009419cellular_componentpilus tip
F0031589biological_processcell-substrate adhesion
F0043709biological_processcell adhesion involved in single-species biofilm formation
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO D 126
ChainResidue
CTHR51
CLEU68
DTHR32
DARG34
DASP48
DHOH129
DHOH135
DHOH194

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO C 206
ChainResidue
CARG135
CILE185
CMET204
CHOH317
CHOH335
CHOH429
CPHE133

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO C 207
ChainResidue
CLYS88
CILE108
DASP11
FHOH272

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO C 208
ChainResidue
CTHR151
CASN164
CALA165
CLEU166
CHOH250
FTRP114
FGLN154

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO F 5
ChainResidue
FPRO104
FALA107
FALA111
FHOH223

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO C 209
ChainResidue
CASP41
CGLY42
CARG110
CHOH339
FHOH312

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO C 210
ChainResidue
CPRO124
CASN191
CASP192
CHOH340
CHOH383

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO C 211
ChainResidue
CPRO124
CASP192
CHOH218
CHOH224
CHOH225

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO F 9
ChainResidue
FLYS64
FGLU152
FHOH253

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO C 212
ChainResidue
CASP41
CALA118
CLYS119
CHOH227
CHOH266
CHOH418

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO D 127
ChainResidue
DPRO62
DPRO92
DLEU93
DTHR94
DHOH294

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO C 213
ChainResidue
CGLN34
CSER35
CPRO53
CLEU54
CHOH357
CHOH364
CHOH365

site_idBC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO F 155
ChainResidue
FPRO48
FPHE49
FGLU98
FASN126
FPHE127
FTYR128
FHOH168

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG C 214
ChainResidue
CTRP36
CGLU38
CLYS44
DASP11

Functional Information from PROSITE/UniProt
site_idPS00635
Number of Residues18
DetailsPILI_CHAPERONE Gram-negative pili assembly chaperone signature. LPqDRESLfWmNVkaIPS
ChainResidueDetails
CLEU75-SER92

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Required for stability and transport => ECO:0000250
ChainResidueDetails
FTYR153

220113

PDB entries from 2024-05-22

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