Functional Information from GO Data
Chain | GOid | namespace | contents |
C | 0005515 | molecular_function | protein binding |
C | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
C | 0042597 | cellular_component | periplasmic space |
C | 0043711 | biological_process | pilus organization |
C | 0044183 | molecular_function | protein folding chaperone |
C | 0061077 | biological_process | chaperone-mediated protein folding |
C | 0071555 | biological_process | cell wall organization |
D | 0009297 | biological_process | pilus assembly |
D | 0015473 | molecular_function | fimbrial usher porin activity |
D | 0016020 | cellular_component | membrane |
F | 0007155 | biological_process | cell adhesion |
F | 0007638 | biological_process | mechanosensory behavior |
F | 0009289 | cellular_component | pilus |
F | 0009419 | cellular_component | pilus tip |
F | 0031589 | biological_process | cell-substrate adhesion |
F | 0043709 | biological_process | cell adhesion involved in single-species biofilm formation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO D 126 |
Chain | Residue |
C | THR51 |
C | LEU68 |
D | THR32 |
D | ARG34 |
D | ASP48 |
D | HOH129 |
D | HOH135 |
D | HOH194 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO C 206 |
Chain | Residue |
C | ARG135 |
C | ILE185 |
C | MET204 |
C | HOH317 |
C | HOH335 |
C | HOH429 |
C | PHE133 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO C 207 |
Chain | Residue |
C | LYS88 |
C | ILE108 |
D | ASP11 |
F | HOH272 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO C 208 |
Chain | Residue |
C | THR151 |
C | ASN164 |
C | ALA165 |
C | LEU166 |
C | HOH250 |
F | TRP114 |
F | GLN154 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO F 5 |
Chain | Residue |
F | PRO104 |
F | ALA107 |
F | ALA111 |
F | HOH223 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO C 209 |
Chain | Residue |
C | ASP41 |
C | GLY42 |
C | ARG110 |
C | HOH339 |
F | HOH312 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO C 210 |
Chain | Residue |
C | PRO124 |
C | ASN191 |
C | ASP192 |
C | HOH340 |
C | HOH383 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO C 211 |
Chain | Residue |
C | PRO124 |
C | ASP192 |
C | HOH218 |
C | HOH224 |
C | HOH225 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO F 9 |
Chain | Residue |
F | LYS64 |
F | GLU152 |
F | HOH253 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO C 212 |
Chain | Residue |
C | ASP41 |
C | ALA118 |
C | LYS119 |
C | HOH227 |
C | HOH266 |
C | HOH418 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO D 127 |
Chain | Residue |
D | PRO62 |
D | PRO92 |
D | LEU93 |
D | THR94 |
D | HOH294 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO C 213 |
Chain | Residue |
C | GLN34 |
C | SER35 |
C | PRO53 |
C | LEU54 |
C | HOH357 |
C | HOH364 |
C | HOH365 |
site_id | BC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO F 155 |
Chain | Residue |
F | PRO48 |
F | PHE49 |
F | GLU98 |
F | ASN126 |
F | PHE127 |
F | TYR128 |
F | HOH168 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PEG C 214 |
Chain | Residue |
C | TRP36 |
C | GLU38 |
C | LYS44 |
D | ASP11 |
Functional Information from PROSITE/UniProt
site_id | PS00635 |
Number of Residues | 18 |
Details | PILI_CHAPERONE Gram-negative pili assembly chaperone signature. LPqDRESLfWmNVkaIPS |
Chain | Residue | Details |
C | LEU75-SER92 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | SITE: Required for stability and transport => ECO:0000250 |
Chain | Residue | Details |
F | TYR153 | |