Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008202 | biological_process | steroid metabolic process |
A | 0010181 | molecular_function | FMN binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0042597 | cellular_component | periplasmic space |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA A 9810 |
Chain | Residue |
A | THR506 |
A | MET507 |
A | GLY508 |
A | GLU534 |
A | THR536 |
A | HOH9826 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE HEC A 801 |
Chain | Residue |
A | LEU24 |
A | SER73 |
A | ALA74 |
A | HIS75 |
A | HOH1005 |
A | HOH1448 |
A | HOH1482 |
A | HOH9978 |
A | HOH9996 |
A | CYS14 |
A | CYS17 |
A | HIS18 |
site_id | AC3 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE HEC A 802 |
Chain | Residue |
A | LEU4 |
A | PHE7 |
A | HIS8 |
A | GLN12 |
A | SER16 |
A | GLN35 |
A | CYS36 |
A | CYS39 |
A | HIS40 |
A | HIS72 |
A | TYR94 |
A | HEC803 |
A | HOH1183 |
A | HOH1325 |
A | HOH1350 |
A | HOH1427 |
A | HOH1701 |
A | HOH1945 |
A | HOH1982 |
site_id | AC4 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE HEC A 803 |
Chain | Residue |
A | HIS40 |
A | LEU43 |
A | HIS52 |
A | ALA57 |
A | HIS58 |
A | VAL66 |
A | ALA67 |
A | CYS68 |
A | CYS71 |
A | HIS72 |
A | PHE90 |
A | ASN91 |
A | MET92 |
A | HEC802 |
A | HEC804 |
A | HOH1475 |
A | HOH1790 |
A | HOH1792 |
A | HOH9918 |
A | HOH9994 |
site_id | AC5 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE HEC A 804 |
Chain | Residue |
A | HIS54 |
A | ASN56 |
A | SER60 |
A | HIS61 |
A | PHE62 |
A | CYS82 |
A | SER84 |
A | CYS85 |
A | HIS86 |
A | PHE88 |
A | LEU167 |
A | GLN338 |
A | VAL374 |
A | LYS431 |
A | LYS434 |
A | TYR435 |
A | HEC803 |
A | HOH1013 |
A | HOH1101 |
A | HOH1170 |
A | HOH1528 |
A | HOH1741 |
A | HOH9845 |
A | HOH9876 |
A | HOH9898 |
site_id | AC6 |
Number of Residues | 44 |
Details | BINDING SITE FOR RESIDUE FAD A 9805 |
Chain | Residue |
A | THR276 |
A | ARG277 |
A | GLY278 |
A | ALA312 |
A | THR313 |
A | GLY314 |
A | THR336 |
A | ASN337 |
A | GLN338 |
A | ASP344 |
A | MET375 |
A | HIS504 |
A | HIS505 |
A | GLY533 |
A | GLU534 |
A | ARG544 |
A | GLY547 |
A | ASN548 |
A | ALA549 |
A | ILE550 |
A | ILE553 |
A | TEO9806 |
A | HOH9812 |
A | HOH9814 |
A | HOH9815 |
A | HOH9816 |
A | HOH9834 |
A | VAL132 |
A | GLY133 |
A | GLY135 |
A | GLY136 |
A | ALA137 |
A | GLU156 |
A | LYS157 |
A | GLU158 |
A | GLY162 |
A | GLY163 |
A | ASN164 |
A | ALA165 |
A | LEU167 |
A | ALA168 |
A | ALA169 |
A | GLY170 |
A | GLY171 |
site_id | AC7 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE TEO A 9806 |
Chain | Residue |
A | ALA169 |
A | GLY170 |
A | MET236 |
A | HIS365 |
A | MET375 |
A | THR377 |
A | GLU378 |
A | ARG402 |
A | HIS504 |
A | ARG544 |
A | GLY546 |
A | GLY547 |
A | FAD9805 |
Functional Information from PROSITE/UniProt
site_id | PS00028 |
Number of Residues | 23 |
Details | ZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. Cvs..ChgtLaevaettkHehynaH |
Chain | Residue | Details |
A | CYS36-HIS58 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | THR377 | |
Chain | Residue | Details |
A | ASN11 | |
A | LEU43 | |
A | VAL46 | |
A | ALA57 | |
A | SER60 | |
Chain | Residue | Details |
A | CYS14 | |
A | CYS36 | |
A | CYS17 | |
A | CYS39 | |
A | CYS68 | |
A | CYS71 | |
A | CYS82 | |
A | CYS85 | |
Chain | Residue | Details |
A | ASP15 | |
A | ASN33 | |
A | ALA47 | |
A | THR50 | |
Chain | Residue | Details |
A | ASP27 | |
A | THR146 | |
A | VAL253 | |
A | THR313 | |
A | SER406 | |
A | PHE480 | |
A | GLY509 | |
A | GLN524 | |
A | VAL525 | |
A | THR49 | |
A | VAL66 | |
A | THR69 | |
A | LYS112 | |
A | VAL131 | |
A | PHE139 | |
A | SER140 | |
A | SER144 | |
Chain | Residue | Details |
A | HIS61 | |
A | HIS8 | |
A | HIS18 | |
A | HIS40 | |
A | HIS58 | |
A | HIS72 | |
A | HIS75 | |
A | HIS86 | |
Chain | Residue | Details |
A | ALA145 | |
A | ALA137 | |
A | GLU156 | |
A | ASN164 | |
A | ALA169 | |
A | GLY170 | |
A | GLY171 | |
A | GLY278 | |
A | ASP344 | |
A | TYR361 | |
A | HIS365 | |
A | GLY340 | |
A | GLU378 | |
A | HIS504 | |
A | HIS505 | |
A | GLU534 | |
A | ARG544 | |
A | GLY547 | |
A | ALA549 | |
A | ILE550 | |
A | ALA352 | |
A | GLY353 | |
A | THR377 | |
A | ASP479 | |
A | MET519 | |
A | LYS522 | |
A | ALA74 | |
Chain | Residue | Details |
A | ARG402 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1d4c |
Chain | Residue | Details |
A | HIS504 | |
A | ARG544 | |
A | HIS365 | |
A | ARG402 | |
site_id | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 20 |
Chain | Residue | Details |
A | HIS365 | increase acidity |
A | GLU378 | proton acceptor, proton donor, proton relay |
A | ARG381 | proton acceptor, proton donor, proton relay |
A | ARG402 | proton acceptor, proton donor |
A | HIS504 | electrostatic stabiliser, proton acceptor, proton donor |
A | HIS505 | electrostatic stabiliser |
A | ARG544 | steric role |