Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
A | 0042597 | cellular_component | periplasmic space |
A | 0043711 | biological_process | pilus organization |
A | 0044183 | molecular_function | protein folding chaperone |
A | 0061077 | biological_process | chaperone-mediated protein folding |
A | 0071555 | biological_process | cell wall organization |
B | 0007155 | biological_process | cell adhesion |
B | 0009289 | cellular_component | pilus |
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 | 0007155 | biological_process | cell adhesion |
D | 0009289 | cellular_component | pilus |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PEG A 301 |
Chain | Residue |
A | PRO124 |
A | LEU150 |
A | ASN191 |
A | ASP192 |
A | HOH422 |
A | HOH428 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PEG A 302 |
Chain | Residue |
A | LEU32 |
A | ILE90 |
A | SER92 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PEG A 303 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEG A 304 |
Chain | Residue |
A | ARG79 |
B | GLN44 |
B | GLU45 |
B | ALA47 |
B | ARG106 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PEG A 305 |
Chain | Residue |
A | LYS119 |
A | MET200 |
A | THR201 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PEG A 306 |
Chain | Residue |
A | ASN73 |
A | GLN77 |
A | PG4307 |
B | GLN57 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PG4 A 307 |
Chain | Residue |
A | ASN25 |
A | ASP26 |
A | PEG306 |
B | ASN59 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 A 308 |
Chain | Residue |
A | MET57 |
A | LYS58 |
A | LYS61 |
C | LYS58 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PEG B 201 |
Chain | Residue |
A | ILE190 |
A | GLY194 |
A | LEU196 |
B | ASN18 |
B | ASP62 |
B | ASN64 |
B | HOH314 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 B 202 |
Chain | Residue |
A | GLY5 |
A | ALA6 |
A | TYR193 |
B | MET17 |
B | ASN18 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PEG C 301 |
Chain | Residue |
C | ASN28 |
C | SER92 |
C | MET93 |
D | ASP29 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PGE C 302 |
Chain | Residue |
A | ASN24 |
C | ASN24 |
C | LYS60 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PGE C 303 |
Chain | Residue |
C | PRO124 |
C | LEU150 |
C | ILE190 |
C | ASN191 |
C | ASP192 |
C | HOH425 |
site_id | BC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PEG C 304 |
site_id | BC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PG4 D 201 |
Chain | Residue |
C | ASN25 |
C | ASP26 |
D | ASP24 |
D | GLY26 |
D | SER27 |
D | ASN59 |
D | ASP60 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PEG D 202 |
Chain | Residue |
C | PRO91 |
C | GLN104 |
D | ASP151 |
D | ALA152 |
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 |
A | LEU75-SER92 | |