Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009297 | biological_process | pilus assembly |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0009297 | biological_process | pilus assembly |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0009297 | biological_process | pilus assembly |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0009297 | biological_process | pilus assembly |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0009297 | biological_process | pilus assembly |
| E | 0016887 | molecular_function | ATP hydrolysis activity |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0009297 | biological_process | pilus assembly |
| F | 0016887 | molecular_function | ATP hydrolysis activity |
| F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 601 |
| Chain | Residue |
| A | CYS458 |
| A | CYS461 |
| A | CYS493 |
| A | CYS496 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | binding site for residue ANP A 602 |
| Chain | Residue |
| A | LYS331 |
| A | THR332 |
| A | VAL333 |
| A | LEU453 |
| A | ARG504 |
| A | TYR508 |
| A | MG603 |
| A | HOH703 |
| A | HOH726 |
| A | HOH727 |
| A | HOH754 |
| A | HOH764 |
| A | HOH769 |
| A | HOH775 |
| A | HOH779 |
| A | LEU300 |
| A | THR327 |
| A | GLY328 |
| A | SER329 |
| A | GLY330 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 603 |
| Chain | Residue |
| A | THR332 |
| A | ANP602 |
| A | HOH703 |
| A | HOH750 |
| A | HOH764 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 601 |
| Chain | Residue |
| B | CYS458 |
| B | CYS461 |
| B | CYS493 |
| B | CYS496 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | binding site for residue ANP B 602 |
| Chain | Residue |
| B | LEU300 |
| B | PRO326 |
| B | THR327 |
| B | GLY328 |
| B | SER329 |
| B | GLY330 |
| B | LYS331 |
| B | THR332 |
| B | VAL333 |
| B | LEU453 |
| B | ARG504 |
| B | TYR508 |
| B | HOH714 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 601 |
| Chain | Residue |
| C | CYS458 |
| C | CYS461 |
| C | CYS493 |
| C | CYS496 |
| site_id | AC7 |
| Number of Residues | 19 |
| Details | binding site for residue ANP C 602 |
| Chain | Residue |
| C | LEU300 |
| C | THR327 |
| C | GLY328 |
| C | SER329 |
| C | GLY330 |
| C | LYS331 |
| C | THR332 |
| C | VAL333 |
| C | HIS420 |
| C | LEU453 |
| C | ARG504 |
| C | TYR508 |
| C | MG603 |
| C | HOH703 |
| C | HOH705 |
| C | HOH722 |
| C | HOH731 |
| C | HOH749 |
| C | HOH750 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 603 |
| Chain | Residue |
| C | THR332 |
| C | ANP602 |
| C | HOH705 |
| C | HOH750 |
| C | HOH764 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 601 |
| Chain | Residue |
| D | CYS458 |
| D | CYS461 |
| D | CYS493 |
| D | CYS496 |
| site_id | AD1 |
| Number of Residues | 12 |
| Details | binding site for residue ANP D 602 |
| Chain | Residue |
| D | LEU300 |
| D | PRO326 |
| D | THR327 |
| D | GLY328 |
| D | SER329 |
| D | GLY330 |
| D | LYS331 |
| D | THR332 |
| D | VAL333 |
| D | LEU453 |
| D | ARG504 |
| D | TYR508 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN E 601 |
| Chain | Residue |
| E | CYS458 |
| E | CYS461 |
| E | CYS493 |
| E | CYS496 |
| site_id | AD3 |
| Number of Residues | 11 |
| Details | binding site for residue ADP E 602 |
| Chain | Residue |
| E | LYS331 |
| E | THR332 |
| E | VAL333 |
| E | ARG504 |
| E | TYR508 |
| E | HOH706 |
| E | LEU300 |
| E | THR327 |
| E | GLY328 |
| E | SER329 |
| E | GLY330 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN F 601 |
| Chain | Residue |
| F | CYS458 |
| F | CYS461 |
| F | CYS493 |
| F | CYS496 |
| site_id | AD5 |
| Number of Residues | 10 |
| Details | binding site for residue ADP F 602 |
| Chain | Residue |
| F | LEU300 |
| F | THR327 |
| F | GLY328 |
| F | SER329 |
| F | GLY330 |
| F | LYS331 |
| F | THR332 |
| F | VAL333 |
| F | TYR508 |
| F | HOH701 |
Functional Information from PROSITE/UniProt
| site_id | PS00662 |
| Number of Residues | 15 |
| Details | T2SP_E Bacterial type II secretion system protein E signature. LRqdPDiIMIGEIRD |
| Chain | Residue | Details |
| A | LEU384-ASP398 | |
