4WVZ
Crystal structure of artificial crosslinked thiol dioxygenase G95C variant from Pseudomonas aeruginosa
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0008198 | molecular_function | ferrous iron binding |
| A | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051213 | molecular_function | dioxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0008198 | molecular_function | ferrous iron binding |
| B | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051213 | molecular_function | dioxygenase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0008198 | molecular_function | ferrous iron binding |
| C | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051213 | molecular_function | dioxygenase activity |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0008198 | molecular_function | ferrous iron binding |
| D | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051213 | molecular_function | dioxygenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue FE2 A 301 |
| Chain | Residue |
| A | HIS89 |
| A | HIS91 |
| A | HIS142 |
| A | HOH402 |
| A | HOH536 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue FE2 B 301 |
| Chain | Residue |
| B | HOH495 |
| B | HIS89 |
| B | HIS91 |
| B | HIS142 |
| B | HOH424 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue FE2 C 301 |
| Chain | Residue |
| C | HIS89 |
| C | HIS91 |
| C | HIS142 |
| C | HOH423 |
| C | HOH526 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue FE2 D 301 |
| Chain | Residue |
| D | HIS89 |
| D | HIS91 |
| D | HIS142 |
| D | HOH455 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | binding site for Di-peptide CYS B 95 and TYR B 159 |
| Chain | Residue |
| B | PHE73 |
| B | SER74 |
| B | HIS91 |
| B | VAL93 |
| B | TRP94 |
| B | LEU96 |
| B | ALA133 |
| B | LEU134 |
| B | HIS157 |
| B | VAL158 |
| B | GLY160 |
| B | ALA161 |
| B | ILE163 |
| B | HOH424 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | binding site for Di-peptide CYS C 95 and TYR C 159 |
| Chain | Residue |
| C | PHE73 |
| C | SER74 |
| C | PHE78 |
| C | HIS91 |
| C | VAL93 |
| C | TRP94 |
| C | LEU96 |
| C | ALA133 |
| C | LEU134 |
| C | HIS157 |
| C | VAL158 |
| C | GLY160 |
| C | ALA161 |
| C | ILE163 |
| C | HOH423 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | binding site for Di-peptide CYS D 95 and TYR D 159 |
| Chain | Residue |
| D | PHE73 |
| D | SER74 |
| D | PHE78 |
| D | HIS91 |
| D | VAL93 |
| D | TRP94 |
| D | LEU96 |
| D | ALA133 |
| D | LEU134 |
| D | HIS157 |
| D | VAL158 |
| D | GLY160 |
| D | ALA161 |
| D | ILE163 |
| D | HOH455 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26272617, ECO:0007744|PDB:3USS |
| Chain | Residue | Details |
| A | HIS89 | |
| D | HIS89 | |
| D | HIS91 | |
| D | HIS142 | |
| A | HIS91 | |
| A | HIS142 | |
| B | HIS89 | |
| B | HIS91 | |
| B | HIS142 | |
| C | HIS89 | |
| C | HIS91 | |
| C | HIS142 |
