6K24
Structure of the Rhodium Mesoporphyrin IX-Reconstituted CYP102A1 Haem Domain with N-Abietoyl-L-Tryptophan
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004497 | molecular_function | monooxygenase activity |
A | 0005506 | molecular_function | iron ion binding |
A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
A | 0020037 | molecular_function | heme binding |
B | 0004497 | molecular_function | monooxygenase activity |
B | 0005506 | molecular_function | iron ion binding |
B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
B | 0020037 | molecular_function | heme binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | binding site for residue WAA A 501 |
Chain | Residue |
A | LEU20 |
A | MET354 |
A | LEU437 |
A | VAL26 |
A | LEU29 |
A | ARG47 |
A | TYR51 |
A | SER72 |
A | GLN73 |
A | ALA74 |
A | LEU188 |
site_id | AC2 |
Number of Residues | 24 |
Details | binding site for residue CV0 A 502 |
Chain | Residue |
A | LYS69 |
A | LEU86 |
A | PHE87 |
A | TRP96 |
A | PHE107 |
A | ALA264 |
A | THR269 |
A | THR327 |
A | PHE331 |
A | PRO392 |
A | PHE393 |
A | GLY394 |
A | ARG398 |
A | ALA399 |
A | CYS400 |
A | ILE401 |
A | GLY402 |
A | DMS503 |
A | HOH603 |
A | HOH609 |
A | HOH625 |
A | HOH655 |
A | HOH668 |
A | HOH678 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue DMS A 503 |
Chain | Residue |
A | PHE87 |
A | ALA264 |
A | THR268 |
A | CV0502 |
site_id | AC4 |
Number of Residues | 12 |
Details | binding site for residue WAA B 501 |
Chain | Residue |
B | LEU20 |
B | PRO25 |
B | VAL26 |
B | LEU29 |
B | ARG47 |
B | TYR51 |
B | SER72 |
B | GLN73 |
B | ALA74 |
B | PHE87 |
B | LEU188 |
B | LEU437 |
site_id | AC5 |
Number of Residues | 26 |
Details | binding site for residue CV0 B 502 |
Chain | Residue |
B | LYS69 |
B | LEU75 |
B | LEU86 |
B | PHE87 |
B | TRP96 |
B | PHE107 |
B | ILE153 |
B | ALA264 |
B | THR268 |
B | THR269 |
B | THR327 |
B | PHE331 |
B | PRO392 |
B | PHE393 |
B | GLY394 |
B | ARG398 |
B | ALA399 |
B | CYS400 |
B | ILE401 |
B | DMS503 |
B | HOH611 |
B | HOH634 |
B | HOH642 |
B | HOH650 |
B | HOH672 |
B | HOH711 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue DMS B 503 |
Chain | Residue |
B | PHE87 |
B | ALA264 |
B | THR268 |
B | CV0502 |
Functional Information from PROSITE/UniProt
site_id | PS00086 |
Number of Residues | 10 |
Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGnGQRACIG |
Chain | Residue | Details |
A | PHE393-GLY402 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15020590, ECO:0007744|PDB:1SMJ |
Chain | Residue | Details |
A | TYR51 | |
B | TYR51 |
Chain | Residue | Details |
A | CYS400 | |
B | CYS400 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Important for catalytic activity => ECO:0000305|PubMed:16403573, ECO:0000305|PubMed:7578081 |
Chain | Residue | Details |
A | THR268 | |
B | THR268 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 699 |
Chain | Residue | Details |
A | THR268 | electrostatic stabiliser, steric role |
A | PHE393 | electrostatic stabiliser, steric role |
A | CYS400 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 699 |
Chain | Residue | Details |
B | THR268 | electrostatic stabiliser, steric role |
B | PHE393 | electrostatic stabiliser, steric role |
B | CYS400 | electrostatic stabiliser |