6K58
Structure of the CYP102A1 Haem Domain with N-Enanthyl-L-Prolyl-L-Phenylalanine
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 | 30 |
| Details | binding site for residue HEM A 501 |
| Chain | Residue |
| A | LYS69 |
| A | THR269 |
| A | LEU322 |
| A | THR327 |
| A | PHE331 |
| A | PRO392 |
| A | PHE393 |
| A | GLY394 |
| A | ARG398 |
| A | ALA399 |
| A | CYS400 |
| A | LEU75 |
| A | ILE401 |
| A | GLY402 |
| A | PHE405 |
| A | ALA406 |
| A | DMS502 |
| A | HOH626 |
| A | HOH657 |
| A | HOH702 |
| A | HOH748 |
| A | HOH822 |
| A | LEU86 |
| A | HOH868 |
| A | PHE87 |
| A | TRP96 |
| A | ILE153 |
| A | ALA264 |
| A | GLY265 |
| A | THR268 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue DMS A 502 |
| Chain | Residue |
| A | PHE87 |
| A | ALA264 |
| A | GLY265 |
| A | THR268 |
| A | HEM501 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue D0L A 503 |
| Chain | Residue |
| A | LEU20 |
| A | ARG47 |
| A | TYR51 |
| A | SER72 |
| A | GLN73 |
| A | ALA74 |
| A | LEU75 |
| A | LEU188 |
| A | MET354 |
| A | LEU437 |
| A | HOH635 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | ASP23 |
| A | PRO25 |
| A | MET185 |
| A | GLN189 |
| A | GLU435 |
| A | THR436 |
| A | HOH603 |
| A | HOH655 |
| A | HOH684 |
| A | HOH713 |
| A | HOH821 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 505 |
| Chain | Residue |
| A | GLU137 |
| A | HIS138 |
| A | GLU140 |
| A | HOH625 |
| A | HOH819 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 506 |
| Chain | Residue |
| A | ILE366 |
| A | ARG378 |
| A | ILE385 |
| A | HOH649 |
| A | HOH786 |
| A | HOH827 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 507 |
| Chain | Residue |
| A | ASN21 |
| A | THR22 |
| A | ASP23 |
| A | ASN186 |
| A | GLN189 |
| A | HOH703 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 508 |
| Chain | Residue |
| A | ASP68 |
| A | HIS92 |
| A | LYS336 |
| A | HOH622 |
| A | HOH731 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 509 |
| Chain | Residue |
| A | GLN387 |
| A | HOH768 |
| B | GLU293 |
| B | ARG296 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 510 |
| Chain | Residue |
| A | HIS100 |
| A | GLY396 |
| A | GLN397 |
| A | ALA399 |
| A | ILE401 |
| A | HOH608 |
| A | HOH657 |
| B | ASN381 |
| site_id | AD2 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 511 |
| Chain | Residue |
| A | TRP130 |
| A | LEU133 |
| A | ASN134 |
| A | ALA135 |
| A | ALA448 |
| A | LYS449 |
| A | SER450 |
| A | HOH601 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 512 |
| Chain | Residue |
| A | LYS9 |
| A | PHE11 |
| A | TYR334 |
| A | GLY350 |
| A | HOH606 |
| A | HOH612 |
| A | HOH745 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 513 |
| Chain | Residue |
| A | ASP121 |
| A | ARG161 |
| A | HOH618 |
| B | GLN128 |
| B | GLU131 |
| B | ARG132 |
| site_id | AD5 |
| Number of Residues | 30 |
| Details | binding site for residue HEM B 501 |
| Chain | Residue |
| B | LYS69 |
| B | LEU75 |
| B | LEU86 |
| B | PHE87 |
| B | TRP96 |
| B | ILE153 |
| B | ALA264 |
| B | GLY265 |
| B | THR268 |
| B | THR269 |
| B | LEU322 |
| B | THR327 |
| B | PHE331 |
| B | PRO392 |
| B | PHE393 |
| B | GLY394 |
| B | ARG398 |
| B | ALA399 |
| B | CYS400 |
| B | ILE401 |
| B | GLY402 |
| B | PHE405 |
| B | ALA406 |
| B | DMS502 |
| B | HOH636 |
| B | HOH669 |
| B | HOH683 |
| B | HOH704 |
| B | HOH767 |
| B | HOH826 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue DMS B 502 |
| Chain | Residue |
| B | PHE87 |
| B | ALA264 |
| B | GLY265 |
| B | THR268 |
| B | HEM501 |
| site_id | AD7 |
| Number of Residues | 10 |
| Details | binding site for residue D0L B 503 |
| Chain | Residue |
| B | LEU20 |
| B | ARG47 |
| B | TYR51 |
| B | SER72 |
| B | GLN73 |
| B | ALA74 |
| B | LEU75 |
| B | LEU188 |
| B | LEU437 |
| B | HOH620 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 504 |
| Chain | Residue |
| B | LYS391 |
| B | GLY394 |
| B | ASN395 |
| B | GLY396 |
| B | GLN403 |
| B | HOH806 |
| site_id | AD9 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 505 |
| Chain | Residue |
| B | ASP23 |
| B | PRO25 |
| B | GLN189 |
| B | GLU435 |
| B | THR436 |
| B | HOH606 |
| B | HOH622 |
| B | HOH676 |
| site_id | AE1 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 506 |
| Chain | Residue |
| B | ILE366 |
| B | ARG378 |
| B | ILE385 |
| B | HOH715 |
| site_id | AE2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 507 |
| Chain | Residue |
| B | ASP68 |
| B | HIS92 |
| B | LYS336 |
| B | HOH613 |
| B | HOH619 |
| site_id | AE3 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 508 |
| Chain | Residue |
| B | ARG79 |
| B | GLY83 |
| B | GLU252 |
| B | HOH682 |
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 |
