6A16
Crystal structure of CYP90B1 in complex with uniconazole
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006694 | biological_process | steroid biosynthetic process |
| A | 0009741 | biological_process | response to brassinosteroid |
| A | 0009753 | biological_process | response to jasmonic acid |
| A | 0009826 | biological_process | unidimensional cell growth |
| A | 0009867 | biological_process | jasmonic acid mediated signaling pathway |
| A | 0010268 | biological_process | brassinosteroid homeostasis |
| A | 0010358 | biological_process | leaf shaping |
| A | 0016020 | cellular_component | membrane |
| A | 0016132 | biological_process | brassinosteroid biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048366 | biological_process | leaf development |
| A | 0080132 | molecular_function | fatty acid 2-hydroxylase activity |
| A | 0160191 | molecular_function | steroid 22S-hydroxylase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | binding site for residue HEM A 601 |
| Chain | Residue |
| A | HIS133 |
| A | PHE455 |
| A | GLY456 |
| A | ARG460 |
| A | CYS462 |
| A | GLY464 |
| A | ALA468 |
| A | UCZ602 |
| A | HOH777 |
| A | HOH780 |
| A | HOH825 |
| A | ARG137 |
| A | HOH852 |
| A | MET188 |
| A | LEU308 |
| A | GLY312 |
| A | THR315 |
| A | ALA319 |
| A | ARG386 |
| A | PRO454 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue UCZ A 602 |
| Chain | Residue |
| A | TYR55 |
| A | TYR112 |
| A | ILE116 |
| A | PHE310 |
| A | ALA311 |
| A | THR315 |
| A | VAL381 |
| A | LEU384 |
| A | HEM601 |
| A | HOH825 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 603 |
| Chain | Residue |
| A | GLN328 |
| A | VAL334 |
| A | ASN484 |
| A | TRP485 |
| A | HOH710 |
| A | HOH745 |
| A | HOH885 |
| A | HOH891 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 604 |
| Chain | Residue |
| A | ASN295 |
| A | CYS330 |
| A | PRO331 |
| A | LYS332 |
| A | PHE425 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue CL A 605 |
| Chain | Residue |
| A | LYS492 |
| A | PHE501 |
| A | PRO502 |
| A | ASN503 |
| A | GLY504 |
| A | LEU505 |
| A | HOH861 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 606 |
| Chain | Residue |
| A | ASP420 |
| A | ARG429 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGgGPRLCAG |
| Chain | Residue | Details |
| A | PHE455-GLY464 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"UniProtKB","id":"P04798","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
