4Y8W
Crystal Structure of Human Cytochrome P450 21A2 Progesterone Complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004497 | molecular_function | monooxygenase activity |
A | 0004509 | molecular_function | steroid 21-monooxygenase activity |
A | 0005496 | molecular_function | steroid binding |
A | 0005506 | molecular_function | iron ion binding |
A | 0005783 | cellular_component | endoplasmic reticulum |
A | 0005789 | cellular_component | endoplasmic reticulum membrane |
A | 0006694 | biological_process | steroid biosynthetic process |
A | 0006704 | biological_process | glucocorticoid biosynthetic process |
A | 0006705 | biological_process | mineralocorticoid biosynthetic process |
A | 0008202 | biological_process | steroid metabolic process |
A | 0008395 | molecular_function | steroid hydroxylase activity |
A | 0016020 | cellular_component | membrane |
A | 0016125 | biological_process | sterol metabolic process |
A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
A | 0020037 | molecular_function | heme binding |
A | 0042445 | biological_process | hormone metabolic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0103069 | molecular_function | 17-hydroxyprogesterone 21-hydroxylase activity |
A | 0106309 | molecular_function | progesterone 21-hydroxylase activity |
B | 0004497 | molecular_function | monooxygenase activity |
B | 0004509 | molecular_function | steroid 21-monooxygenase activity |
B | 0005496 | molecular_function | steroid binding |
B | 0005506 | molecular_function | iron ion binding |
B | 0005783 | cellular_component | endoplasmic reticulum |
B | 0005789 | cellular_component | endoplasmic reticulum membrane |
B | 0006694 | biological_process | steroid biosynthetic process |
B | 0006704 | biological_process | glucocorticoid biosynthetic process |
B | 0006705 | biological_process | mineralocorticoid biosynthetic process |
B | 0008202 | biological_process | steroid metabolic process |
B | 0008395 | molecular_function | steroid hydroxylase activity |
B | 0016020 | cellular_component | membrane |
B | 0016125 | biological_process | sterol metabolic process |
B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
B | 0020037 | molecular_function | heme binding |
B | 0042445 | biological_process | hormone metabolic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0103069 | molecular_function | 17-hydroxyprogesterone 21-hydroxylase activity |
B | 0106309 | molecular_function | progesterone 21-hydroxylase activity |
C | 0004497 | molecular_function | monooxygenase activity |
C | 0004509 | molecular_function | steroid 21-monooxygenase activity |
C | 0005496 | molecular_function | steroid binding |
C | 0005506 | molecular_function | iron ion binding |
C | 0005783 | cellular_component | endoplasmic reticulum |
C | 0005789 | cellular_component | endoplasmic reticulum membrane |
C | 0006694 | biological_process | steroid biosynthetic process |
C | 0006704 | biological_process | glucocorticoid biosynthetic process |
C | 0006705 | biological_process | mineralocorticoid biosynthetic process |
C | 0008202 | biological_process | steroid metabolic process |
C | 0008395 | molecular_function | steroid hydroxylase activity |
C | 0016020 | cellular_component | membrane |
C | 0016125 | biological_process | sterol metabolic process |
C | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
C | 0020037 | molecular_function | heme binding |
C | 0042445 | biological_process | hormone metabolic process |
C | 0046872 | molecular_function | metal ion binding |
C | 0103069 | molecular_function | 17-hydroxyprogesterone 21-hydroxylase activity |
C | 0106309 | molecular_function | progesterone 21-hydroxylase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 20 |
Details | binding site for residue HEM A 603 |
Chain | Residue |
A | ARG92 |
A | VAL360 |
A | LEU364 |
A | HIS366 |
A | LEU389 |
A | ALA421 |
A | PHE422 |
A | ARG427 |
A | CYS429 |
A | LEU430 |
A | GLY431 |
A | SER109 |
A | STR604 |
A | TRP117 |
A | LYS121 |
A | ILE173 |
A | GLY292 |
A | GLY293 |
A | THR296 |
A | VAL359 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue STR A 604 |
Chain | Residue |
A | SER109 |
A | VAL198 |
A | TRP202 |
A | ARG234 |
A | ASP288 |
A | GLY292 |
A | LEU364 |
A | VAL470 |
A | HEM603 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 601 |
Chain | Residue |
B | ARG61 |
C | LYS99 |
C | ARG103 |
C | ARG217 |
site_id | AC4 |
Number of Residues | 20 |
Details | binding site for residue HEM B 602 |
Chain | Residue |
B | ARG92 |
B | SER109 |
B | TRP117 |
B | LYS121 |
B | ILE173 |
B | GLY292 |
B | GLY293 |
B | THR296 |
B | THR300 |
B | VAL360 |
B | LEU364 |
B | HIS366 |
B | LEU389 |
B | ALA421 |
B | PHE422 |
B | ARG427 |
B | CYS429 |
B | LEU430 |
B | GLY431 |
B | STR603 |
site_id | AC5 |
Number of Residues | 8 |
Details | binding site for residue STR B 603 |
Chain | Residue |
B | VAL101 |
B | SER109 |
B | VAL198 |
B | TRP202 |
B | ARG234 |
B | ASP288 |
B | LEU364 |
B | HEM602 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue SO4 C 601 |
Chain | Residue |
B | LEU96 |
B | LYS99 |
B | ARG103 |
B | ARG217 |
C | ARG61 |
site_id | AC7 |
Number of Residues | 20 |
Details | binding site for residue HEM C 602 |
Chain | Residue |
C | ARG92 |
C | SER109 |
C | TRP117 |
C | LYS121 |
C | ILE173 |
C | LEU289 |
C | GLY292 |
C | GLY293 |
C | THR296 |
C | THR300 |
C | VAL359 |
C | VAL360 |
C | HIS366 |
C | LEU389 |
C | ALA421 |
C | PHE422 |
C | ARG427 |
C | CYS429 |
C | LEU430 |
C | GLY431 |
site_id | AC8 |
Number of Residues | 7 |
Details | binding site for residue STR C 603 |
Chain | Residue |
C | SER109 |
C | VAL198 |
C | TRP202 |
C | ILE231 |
C | ARG234 |
C | ASP288 |
C | LEU364 |
site_id | AC9 |
Number of Residues | 10 |
Details | binding site for residues SO4 A 601 and SO4 A 602 |
Chain | Residue |
A | ARG103 |
A | ARG103 |
A | ARG217 |
A | ARG217 |
A | ARG61 |
A | ARG61 |
A | LEU96 |
A | LEU96 |
A | LYS99 |
A | LYS99 |
site_id | AD1 |
Number of Residues | 10 |
Details | binding site for residues SO4 A 601 and SO4 A 602 |
Chain | Residue |
A | ARG61 |
A | ARG61 |
A | LEU96 |
A | LEU96 |
A | LYS99 |
A | LYS99 |
A | ARG103 |
A | ARG103 |
A | ARG217 |
A | ARG217 |
site_id | AD2 |
Number of Residues | 10 |
Details | binding site for residues SO4 A 601 and SO4 A 602 |
Chain | Residue |
A | ARG61 |
A | ARG61 |
A | LEU96 |
A | LEU96 |
A | LYS99 |
A | LYS99 |
A | ARG103 |
A | ARG103 |
A | ARG217 |
A | ARG217 |
site_id | AD3 |
Number of Residues | 10 |
Details | binding site for residues SO4 A 601 and SO4 A 602 |
Chain | Residue |
A | ARG61 |
A | ARG61 |
A | LEU96 |
A | LEU96 |
A | LYS99 |
A | LYS99 |
A | ARG103 |
A | ARG103 |
A | ARG217 |
A | ARG217 |
site_id | AD4 |
Number of Residues | 10 |
Details | binding site for residues SO4 A 601 and SO4 A 602 |
Chain | Residue |
A | ARG61 |
A | ARG61 |
A | LEU96 |
A | LEU96 |
A | LYS99 |
A | LYS99 |
A | ARG103 |
A | ARG103 |
A | ARG217 |
A | ARG217 |
site_id | AD5 |
Number of Residues | 10 |
Details | binding site for residues SO4 A 601 and SO4 A 602 |
Chain | Residue |
A | ARG61 |
A | ARG61 |
A | LEU96 |
A | LEU96 |
A | LYS99 |
A | LYS99 |
A | ARG103 |
A | ARG103 |
A | ARG217 |
A | ARG217 |
Functional Information from PROSITE/UniProt
site_id | PS00086 |
Number of Residues | 10 |
Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGcGARVCLG |
Chain | Residue | Details |
A | PHE422-GLY431 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 15 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25855791, ECO:0007744|PDB:4Y8W |
Chain | Residue | Details |
A | ARG92 | |
B | ARG427 | |
C | ARG92 | |
C | LYS121 | |
C | ARG234 | |
C | HIS366 | |
C | ARG427 | |
A | LYS121 | |
A | ARG234 | |
A | HIS366 | |
A | ARG427 | |
B | ARG92 | |
B | LYS121 | |
B | ARG234 | |
B | HIS366 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: axial binding residue => ECO:0000269|PubMed:25855791, ECO:0007744|PDB:4Y8W |
Chain | Residue | Details |
A | CYS429 | |
B | CYS429 | |
C | CYS429 |