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 |
H | 0007155 | biological_process | cell adhesion |
H | 0009289 | cellular_component | pilus |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO C 2011 |
Chain | Residue |
C | ALA6 |
C | THR7 |
C | ARG8 |
C | ASP192 |
C | TYR193 |
C | GLY194 |
H | THR158 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO H 2012 |
Chain | Residue |
H | CYS161 |
H | ASP162 |
H | CYS187 |
H | ALA188 |
H | HOH2063 |
H | HOH2078 |
C | ALA3 |
H | GLY160 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO C 2013 |
Chain | Residue |
C | PRO124 |
C | ASP192 |
C | EDO2015 |
C | HOH2035 |
C | HOH2049 |
C | HOH2093 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO C 2014 |
Chain | Residue |
C | LYS119 |
C | LEU120 |
C | PRO123 |
C | HOH2222 |
C | HOH2233 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO C 2015 |
Chain | Residue |
C | PRO124 |
C | ASN191 |
C | ASP192 |
C | TYR193 |
C | EDO2013 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO C 2016 |
Chain | Residue |
C | VAL2 |
C | LEU4 |
C | VAL87 |
C | ALA89 |
C | ILE107 |
C | SER109 |
C | HOH2038 |
H | EDO2017 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO H 2017 |
Chain | Residue |
C | VAL2 |
C | SER109 |
C | EDO2016 |
H | CYS161 |
H | PHE276 |
H | TYR278 |
H | HOH2024 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO D 2019 |
Chain | Residue |
D | ARG47 |
D | THR50 |
D | HOH2136 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO H 2021 |
Chain | Residue |
C | ASN28 |
C | SER29 |
C | GLY158 |
H | ASP167 |
H | HOH2048 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO C 2022 |
Chain | Residue |
C | MET204 |
C | GLU205 |
D | ALA77 |
D | VAL79 |
D | ALA80 |
site_id | BC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO C 2023 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO C 2024 |
Chain | Residue |
C | GLN17 |
C | GLU18 |
C | GLN19 |
C | HOH2230 |
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 | |