6PD1
PntC-AEPT: fusion protein of phosphonate-specific cytidylyltransferase and 2-aminoethylphosphonate (AEP) transaminase from Treponema denticola
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0019700 | biological_process | organic phosphonate catabolic process |
| A | 0032923 | biological_process | organic phosphonate biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047304 | molecular_function | 2-aminoethylphosphonate-pyruvate transaminase activity |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0019700 | biological_process | organic phosphonate catabolic process |
| B | 0032923 | biological_process | organic phosphonate biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047304 | molecular_function | 2-aminoethylphosphonate-pyruvate transaminase activity |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0016779 | molecular_function | nucleotidyltransferase activity |
| C | 0019700 | biological_process | organic phosphonate catabolic process |
| C | 0032923 | biological_process | organic phosphonate biosynthetic process |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0047304 | molecular_function | 2-aminoethylphosphonate-pyruvate transaminase activity |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0016779 | molecular_function | nucleotidyltransferase activity |
| D | 0019700 | biological_process | organic phosphonate catabolic process |
| D | 0032923 | biological_process | organic phosphonate biosynthetic process |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0047304 | molecular_function | 2-aminoethylphosphonate-pyruvate transaminase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 701 |
| Chain | Residue |
| A | GLU104 |
| A | ASP106 |
| A | GLU220 |
| A | HOH849 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 702 |
| Chain | Residue |
| A | GLU49 |
| A | ALA71 |
| A | LEU504 |
| A | LYS507 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 703 |
| Chain | Residue |
| A | LEU296 |
| A | PRO424 |
| A | MET425 |
| A | PHE294 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 704 |
| Chain | Residue |
| A | LYS123 |
| A | ASN124 |
| A | PRO207 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 705 |
| Chain | Residue |
| A | GLN285 |
| A | CYS288 |
| A | GLU306 |
| A | THR307 |
| A | PHE481 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 706 |
| Chain | Residue |
| A | SER313 |
| A | GLY314 |
| A | THR315 |
| A | TYR340 |
| A | ARG343 |
| C | PHE489 |
| C | THR490 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue MG B 701 |
| Chain | Residue |
| B | GLU104 |
| B | ASP106 |
| B | GLU220 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 702 |
| Chain | Residue |
| B | LEU293 |
| B | PHE294 |
| B | ALA295 |
| B | LEU296 |
| B | MET425 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 703 |
| Chain | Residue |
| B | GLN285 |
| B | CYS288 |
| B | GLU306 |
| B | THR307 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 704 |
| Chain | Residue |
| B | SER313 |
| B | GLY314 |
| B | THR315 |
| B | TYR340 |
| D | THR490 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 705 |
| Chain | Residue |
| B | TYR575 |
| B | LYS578 |
| B | ARG586 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 706 |
| Chain | Residue |
| B | CYS288 |
| B | MET309 |
| B | GLN477 |
| B | PHE481 |
| B | THR487 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 1102 |
| Chain | Residue |
| C | LYS25 |
| C | GLU104 |
| C | ASP106 |
| C | GLU220 |
| C | HOH1225 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 C 1103 |
| Chain | Residue |
| A | PHE489 |
| A | THR490 |
| C | SER313 |
| C | GLY314 |
| C | THR315 |
| C | TYR340 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO C 1104 |
| Chain | Residue |
| C | CYS288 |
| C | VAL308 |
| C | MET309 |
| C | GLN477 |
| C | THR487 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue GOL C 1105 |
| Chain | Residue |
| C | TYR340 |
| C | ARG343 |
| C | THR390 |
| C | TYR575 |
| C | LYS578 |
| C | ARG586 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue NI C 1106 |
| Chain | Residue |
| C | HIS620 |
| C | HIS622 |
| D | ASP349 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 C 1107 |
| Chain | Residue |
| C | MET1 |
| C | LYS3 |
| C | ALA279 |
| C | ASP282 |
| C | LEU283 |
| site_id | AE1 |
| Number of Residues | 3 |
| Details | binding site for residue MG D 701 |
| Chain | Residue |
| D | GLU104 |
| D | ASP106 |
| D | GLU220 |
| site_id | AE2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO D 702 |
| Chain | Residue |
| D | CYS288 |
| D | VAL308 |
| D | MET309 |
| D | GLN477 |
| D | PHE481 |
| site_id | AE3 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 D 703 |
| Chain | Residue |
| B | PHE489 |
| B | THR490 |
| D | SER313 |
| D | GLY314 |
| D | THR315 |
| D | TYR340 |
| site_id | AE4 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 D 704 |
| Chain | Residue |
| D | ILE357 |
| C | GLU618 |
| D | ALA345 |
| D | ASP349 |
| site_id | AE5 |
| Number of Residues | 8 |
| Details | binding site for Di-peptide EDO C 1101 and ARG C 248 |
| Chain | Residue |
| A | ILE118 |
| A | ASN119 |
| A | ASP120 |
| A | ALA271 |
| C | VAL247 |
| C | ARG249 |
| C | GLU250 |
| C | HOH1212 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 80 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:31420548, ECO:0007744|PDB:6PD2 |
| Chain | Residue | Details |
| A | LEU8 | |
| A | ASP136 | |
| A | LYS153 | |
| A | GLU196 | |
| A | GLU220 | |
| A | ASP222 | |
| A | SER313 | |
| A | GLY314 | |
| A | THR315 | |
| A | THR390 | |
| A | LYS441 | |
| A | GLY10 | |
| A | THR490 | |
| B | LEU8 | |
| B | GLY10 | |
| B | GLY11 | |
| B | LYS25 | |
| B | THR83 | |
| B | THR88 | |
| B | GLU104 | |
| B | SER105 | |
| B | ASP106 | |
| A | GLY11 | |
| B | ASP136 | |
| B | LYS153 | |
| B | GLU196 | |
| B | GLU220 | |
| B | ASP222 | |
| B | SER313 | |
| B | GLY314 | |
| B | THR315 | |
| B | THR390 | |
| B | LYS441 | |
| A | LYS25 | |
| B | THR490 | |
| C | LEU8 | |
| C | GLY10 | |
| C | GLY11 | |
| C | LYS25 | |
| C | THR83 | |
| C | THR88 | |
| C | GLU104 | |
| C | SER105 | |
| C | ASP106 | |
| A | THR83 | |
| C | ASP136 | |
| C | LYS153 | |
| C | GLU196 | |
| C | GLU220 | |
| C | ASP222 | |
| C | SER313 | |
| C | GLY314 | |
| C | THR315 | |
| C | THR390 | |
| C | LYS441 | |
| A | THR88 | |
| C | THR490 | |
| D | LEU8 | |
| D | GLY10 | |
| D | GLY11 | |
| D | LYS25 | |
| D | THR83 | |
| D | THR88 | |
| D | GLU104 | |
| D | SER105 | |
| D | ASP106 | |
| A | GLU104 | |
| D | ASP136 | |
| D | LYS153 | |
| D | GLU196 | |
| D | GLU220 | |
| D | ASP222 | |
| D | SER313 | |
| D | GLY314 | |
| D | THR315 | |
| D | THR390 | |
| D | LYS441 | |
| A | SER105 | |
| D | THR490 | |
| A | ASP106 |
