2V3A
Crystal structure of rubredoxin reductase from Pseudomonas aeruginosa.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0015044 | molecular_function | rubredoxin-NAD+ reductase activity |
| A | 0015046 | molecular_function | rubredoxin-NADP+ reductase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0043448 | biological_process | alkane catabolic process |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG A1385 |
| Chain | Residue |
| A | LEU184 |
| A | VAL317 |
| A | HOH2218 |
| A | HOH2219 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG A1386 |
| Chain | Residue |
| A | MET290 |
| A | PRO314 |
| A | ASN376 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG A1387 |
| Chain | Residue |
| A | LEU185 |
| A | HIS186 |
| A | TRP339 |
| A | GLY183 |
| A | LEU184 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG A1388 |
| Chain | Residue |
| A | SER264 |
| A | ARG266 |
| A | PRO307 |
| A | GLN309 |
| A | HOH2220 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG A1389 |
| Chain | Residue |
| A | ARG82 |
| A | ARG244 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PEG A1390 |
| Chain | Residue |
| A | ARG82 |
| A | VAL83 |
| A | ARG115 |
| A | PRO117 |
| A | GLU246 |
| A | LEU247 |
| A | HOH2221 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A1391 |
| Chain | Residue |
| A | LEU155 |
| A | ILE156 |
| A | HOH2130 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A1392 |
| Chain | Residue |
| A | ARG242 |
| A | THR245 |
| A | GLU246 |
| A | ARG257 |
| site_id | AC9 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE FAD A1393 |
| Chain | Residue |
| A | ILE10 |
| A | GLY11 |
| A | THR12 |
| A | GLY13 |
| A | LEU14 |
| A | ALA15 |
| A | THR36 |
| A | ALA37 |
| A | ASP38 |
| A | LYS45 |
| A | PRO46 |
| A | THR81 |
| A | ARG82 |
| A | VAL83 |
| A | ALA108 |
| A | TRP109 |
| A | GLY110 |
| A | ILE156 |
| A | GLU159 |
| A | PHE160 |
| A | GLY276 |
| A | ASP277 |
| A | LEU287 |
| A | TYR288 |
| A | VAL289 |
| A | LEU292 |
| A | LYS320 |
| A | HOH2022 |
| A | HOH2091 |
| A | HOH2156 |
| A | HOH2222 |
| A | HOH2223 |
| A | HOH2224 |
| A | HOH2226 |
| A | HOH2227 |
| A | HOH2228 |
| A | HOH2229 |
| A | HOH2230 |
| A | HOH2231 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17636129","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2V3A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2V3B","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
