5D3U
Crystal structure of the 5-selective H176F mutant of Cytochrome TxtE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| 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 |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | binding site for residue HEM A 501 |
| Chain | Residue |
| A | ARG59 |
| A | SER254 |
| A | THR296 |
| A | ARG298 |
| A | SER349 |
| A | GLY351 |
| A | VAL354 |
| A | HIS355 |
| A | CYS357 |
| A | ALA359 |
| A | ILE363 |
| A | VAL87 |
| A | TRP502 |
| A | HOH688 |
| A | HOH787 |
| A | MET88 |
| A | HIS95 |
| A | ARG99 |
| A | PHE155 |
| A | ALA245 |
| A | THR250 |
| A | THR251 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue TRP A 502 |
| Chain | Residue |
| A | ARG59 |
| A | MET88 |
| A | TYR89 |
| A | PHE176 |
| A | ASN293 |
| A | THR296 |
| A | TRP297 |
| A | PHE395 |
| A | HEM501 |
| A | HOH664 |
| A | HOH671 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | ARG264 |
| A | PRO266 |
| A | ARG267 |
| A | HOH658 |
| B | ASP15 |
| B | TYR289 |
| B | ARG326 |
| B | GOL503 |
| B | HOH994 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | binding site for residue HEM B 501 |
| Chain | Residue |
| B | ARG59 |
| B | VAL87 |
| B | MET88 |
| B | HIS95 |
| B | ARG99 |
| B | PHE155 |
| B | ALA245 |
| B | THR250 |
| B | THR251 |
| B | SER254 |
| B | THR296 |
| B | ARG298 |
| B | SER349 |
| B | GLY351 |
| B | VAL354 |
| B | HIS355 |
| B | CYS357 |
| B | ALA359 |
| B | TRP502 |
| B | HOH622 |
| B | HOH671 |
| B | HOH773 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | binding site for residue TRP B 502 |
| Chain | Residue |
| B | ARG59 |
| B | MET88 |
| B | TYR89 |
| B | PHE176 |
| B | ASN293 |
| B | THR296 |
| B | TRP297 |
| B | PHE395 |
| B | HEM501 |
| B | HOH622 |
| B | HOH686 |
| B | HOH698 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| A | ARG267 |
| A | GOL503 |
| B | PRO14 |
| B | TYR17 |
| B | ARG264 |
| B | TYR289 |
| B | ASN290 |
| B | ARG326 |
| B | TRP389 |
| B | ARG396 |
| B | CL504 |
| B | HOH689 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 504 |
| Chain | Residue |
| B | ARG264 |
| B | TYR289 |
| B | GOL503 |
| B | HOH788 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGqGVHACLA |
| Chain | Residue | Details |
| A | PHE350-ALA359 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25182183","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27102675","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4TPO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5D3U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5D40","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25182183","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27102675","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24282603","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4L36","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TPN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TPO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5D3U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5D40","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27102675","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5D3U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5D40","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"25182183","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27102675","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24282603","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4L36","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TPN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TPO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5D3U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5D40","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
