3DKQ
Crystal structure of Putative Oxygenase (YP_001051978.1) from SHEWANELLA BALTICA OS155 at 2.26 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0006879 | biological_process | intracellular iron ion homeostasis |
| A | 0006974 | biological_process | DNA damage response |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| A | 0031418 | molecular_function | L-ascorbic acid binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051213 | molecular_function | dioxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0006879 | biological_process | intracellular iron ion homeostasis |
| B | 0006974 | biological_process | DNA damage response |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| B | 0031418 | molecular_function | L-ascorbic acid binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051213 | molecular_function | dioxygenase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0006879 | biological_process | intracellular iron ion homeostasis |
| C | 0006974 | biological_process | DNA damage response |
| C | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| C | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| C | 0031418 | molecular_function | L-ascorbic acid binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051213 | molecular_function | dioxygenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NI A 500 |
| Chain | Residue |
| A | HIS96 |
| A | ASP98 |
| A | HIS157 |
| A | IMD501 |
| A | IMD502 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NI B 500 |
| Chain | Residue |
| B | HOH551 |
| B | HIS96 |
| B | ASP98 |
| B | HIS157 |
| B | IMD501 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NI C 500 |
| Chain | Residue |
| C | HIS96 |
| C | ASP98 |
| C | HIS157 |
| C | IMD501 |
| C | IMD502 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE IMD A 501 |
| Chain | Residue |
| A | SER33 |
| A | GLY34 |
| A | HIS96 |
| A | ASP98 |
| A | TRP173 |
| A | NI500 |
| A | IMD502 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE IMD A 502 |
| Chain | Residue |
| A | PHE93 |
| A | HIS96 |
| A | LEU130 |
| A | TYR151 |
| A | HIS157 |
| A | VAL159 |
| A | NI500 |
| A | IMD501 |
| A | HOH545 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE IMD B 501 |
| Chain | Residue |
| B | TYR87 |
| B | PHE93 |
| B | HIS96 |
| B | TYR151 |
| B | HIS157 |
| B | VAL159 |
| B | NI500 |
| B | HOH520 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE IMD C 501 |
| Chain | Residue |
| C | PHE93 |
| C | HIS96 |
| C | ASP98 |
| C | TRP173 |
| C | NI500 |
| C | IMD502 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE IMD C 502 |
| Chain | Residue |
| C | PHE93 |
| C | HIS96 |
| C | TYR151 |
| C | HIS157 |
| C | VAL159 |
| C | NI500 |
| C | IMD501 |
| C | HOH504 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE IMD B 502 |
| Chain | Residue |
| A | GLN138 |
| A | SER140 |
| B | GLU123 |
| B | ASN124 |
| B | TYR125 |
| B | GLN126 |
| B | SER164 |
| B | GLY165 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C 503 |
| Chain | Residue |
| A | ASP180 |
| A | GLN183 |
| A | GOL503 |
| B | ARG220 |
| C | ASP180 |
| C | ARG220 |
| C | HOH537 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 503 |
| Chain | Residue |
| A | ARG179 |
| C | GLN183 |
| C | ARG220 |
| C | TRP221 |
| C | GOL503 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 504 |
| Chain | Residue |
| A | GLN183 |
| A | ARG220 |
| A | GLU223 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 505 |
| Chain | Residue |
| A | ILE97 |
| A | GLN133 |
| A | SER154 |
| A | HOH619 |
| C | PHE208 |
| C | ASN209 |
| site_id | BC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 506 |
| Chain | Residue |
| A | GLY0 |
| A | MSE1 |
| A | LEU2 |
| A | ILE132 |
| A | ASP134 |
| A | TYR136 |
| A | GLY137 |
| A | GLN138 |
| A | GLN139 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 507 |
| Chain | Residue |
| A | ASP191 |
| A | GLN195 |
| A | SER211 |
| A | TYR214 |
| A | HIS215 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00657 |
| Chain | Residue | Details |
| A | HIS96 | |
| A | ASP98 | |
| A | HIS157 | |
| C | ASP98 | |
| C | HIS157 | |
| C | ARG167 | |
| A | ARG167 | |
| B | HIS96 | |
| B | ASP98 | |
| B | HIS157 | |
| B | ARG167 | |
| C | HIS96 |
