2AHR
Crystal Structures of 1-Pyrroline-5-Carboxylate Reductase from Human Pathogen Streptococcus pyogenes
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004735 | molecular_function | pyrroline-5-carboxylate reductase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0055129 | biological_process | L-proline biosynthetic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004735 | molecular_function | pyrroline-5-carboxylate reductase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0055129 | biological_process | L-proline biosynthetic process |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004735 | molecular_function | pyrroline-5-carboxylate reductase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0055129 | biological_process | L-proline biosynthetic process |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004735 | molecular_function | pyrroline-5-carboxylate reductase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0008652 | biological_process | amino acid biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0055129 | biological_process | L-proline biosynthetic process |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0004735 | molecular_function | pyrroline-5-carboxylate reductase activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0008652 | biological_process | amino acid biosynthetic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0055129 | biological_process | L-proline biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NA A 1257 |
| Chain | Residue |
| A | GLY89 |
| A | ARG94 |
| A | ALA253 |
| A | LYS254 |
| A | LEU256 |
| A | HOH1509 |
| A | HOH1579 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NA B 1258 |
| Chain | Residue |
| B | ALA253 |
| B | LYS254 |
| B | LEU256 |
| B | HOH1511 |
| B | HOH1566 |
| B | GLY89 |
| B | ARG94 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA C 1259 |
| Chain | Residue |
| C | GLY89 |
| C | ALA253 |
| C | LYS254 |
| C | LEU256 |
| C | HOH1511 |
| C | HOH1574 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NA D 1260 |
| Chain | Residue |
| D | GLY89 |
| D | ARG94 |
| D | ALA253 |
| D | LYS254 |
| D | LEU256 |
| D | HOH1656 |
| D | HOH1657 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NA E 1261 |
| Chain | Residue |
| E | GLY89 |
| E | ARG94 |
| E | ALA253 |
| E | LYS254 |
| E | LEU256 |
| E | HOH1583 |
| E | HOH1590 |
| site_id | AC6 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAP A 1500 |
| Chain | Residue |
| A | GLY7 |
| A | VAL8 |
| A | GLY9 |
| A | LYS10 |
| A | MSE11 |
| A | GLY30 |
| A | SER31 |
| A | ARG35 |
| A | HIS51 |
| A | GLY64 |
| A | ILE65 |
| A | LYS66 |
| A | PRO67 |
| A | LEU69 |
| A | VAL73 |
| A | MSE86 |
| A | ALA87 |
| A | ALA88 |
| A | MSE109 |
| A | PRO110 |
| A | MSE112 |
| A | HOH1527 |
| A | HOH1529 |
| A | HOH1574 |
| A | HOH1578 |
| A | HOH1605 |
| A | HOH1635 |
| A | HOH1637 |
| A | HOH1646 |
| D | ALA218 |
| D | ILE219 |
| D | SER221 |
| D | HOH1637 |
| site_id | AC7 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAP B 1501 |
| Chain | Residue |
| B | GLY7 |
| B | VAL8 |
| B | GLY9 |
| B | LYS10 |
| B | MSE11 |
| B | GLY30 |
| B | SER31 |
| B | ARG35 |
| B | HIS51 |
| B | GLY64 |
| B | ILE65 |
| B | LYS66 |
| B | PRO67 |
| B | LEU69 |
| B | MSE86 |
| B | ALA87 |
| B | ALA88 |
| B | MSE109 |
| B | PRO110 |
| B | HOH1520 |
| B | HOH1535 |
| B | HOH1586 |
| B | HOH1589 |
| B | HOH1632 |
| C | ILE219 |
| C | SER221 |
| site_id | AC8 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAP C 1502 |
| Chain | Residue |
| C | GLY9 |
| C | LYS10 |
| C | MSE11 |
| C | GLY30 |
| C | SER31 |
| C | ARG35 |
| C | HIS51 |
| C | GLY64 |
| C | ILE65 |
| C | LYS66 |
| C | PRO67 |
| C | VAL73 |
| C | MSE86 |
| C | ALA87 |
| C | ALA88 |
| C | MSE109 |
| C | PRO110 |
| C | MSE112 |
| C | HOH1525 |
| C | HOH1533 |
| C | HOH1580 |
| C | HOH1601 |
| B | ALA218 |
| B | ILE219 |
| B | SER221 |
| B | PRO222 |
| B | HOH1628 |
| C | VAL8 |
| site_id | AC9 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAP D 1503 |
| Chain | Residue |
| A | ALA218 |
| A | ILE219 |
| A | SER221 |
| D | GLY7 |
| D | VAL8 |
| D | GLY9 |
| D | LYS10 |
| D | MSE11 |
| D | GLY30 |
| D | SER31 |
| D | ARG35 |
| D | HIS51 |
| D | GLY64 |
| D | ILE65 |
| D | LYS66 |
| D | PRO67 |
| D | LEU69 |
| D | VAL73 |
| D | MSE86 |
| D | ALA87 |
| D | ALA88 |
| D | MSE109 |
| D | PRO110 |
| D | MSE112 |
| D | HOH1517 |
| D | HOH1520 |
| D | HOH1521 |
| D | HOH1577 |
| D | HOH1594 |
| D | HOH1614 |
| D | HOH1617 |
| D | HOH1648 |
| D | HOH1660 |
| site_id | BC1 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAP E 1504 |
| Chain | Residue |
| E | GLY7 |
| E | GLY9 |
| E | LYS10 |
| E | MSE11 |
| E | GLY30 |
| E | SER31 |
| E | ARG35 |
| E | HIS51 |
| E | GLY64 |
| E | ILE65 |
| E | LYS66 |
| E | PRO67 |
| E | LEU69 |
| E | MSE86 |
| E | ALA87 |
| E | ALA88 |
| E | MSE109 |
| E | PRO110 |
| E | MSE112 |
| E | ILE219 |
| E | SER221 |
| E | HOH1517 |
| E | HOH1554 |
| E | HOH1596 |
| E | HOH1606 |
| E | HOH1629 |
| E | HOH1632 |
| E | HOH1633 |
| E | HOH1664 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE FMT A 1508 |
| Chain | Residue |
| A | ASP251 |
| A | LYS254 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT B 1509 |
| Chain | Residue |
| B | ILE250 |
| B | ASP251 |
| B | LYS254 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT C 1510 |
| Chain | Residue |
| B | ASN183 |
| C | ILE250 |
| C | ASP251 |
| C | LYS254 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT D 1511 |
| Chain | Residue |
| D | ILE250 |
| D | ASP251 |
| D | LYS254 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT E 1512 |
| Chain | Residue |
| E | ILE250 |
| E | ASP251 |
| E | LYS254 |
