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 | 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 | 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 | 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 | |
C | ASP98 | |
C | HIS157 | |
C | ARG167 | |
A | ASP98 | |
A | HIS157 | |
A | ARG167 | |
B | HIS96 | |
B | ASP98 | |
B | HIS157 | |
B | ARG167 | |
C | HIS96 |