4H6Q
Structure of oxidized Deinococcus radiodurans proline dehydrogenase complexed with L-tetrahydrofuroic acid
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004657 | molecular_function | proline dehydrogenase activity |
| A | 0006560 | biological_process | proline metabolic process |
| A | 0006562 | biological_process | proline catabolic process |
| A | 0010133 | biological_process | proline catabolic process to glutamate |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0071949 | molecular_function | FAD binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004657 | molecular_function | proline dehydrogenase activity |
| C | 0006560 | biological_process | proline metabolic process |
| C | 0006562 | biological_process | proline catabolic process |
| C | 0010133 | biological_process | proline catabolic process to glutamate |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE FAD A 2001 |
| Chain | Residue |
| A | ASP135 |
| A | TYR193 |
| A | ALA228 |
| A | THR229 |
| A | HIS230 |
| A | ASP231 |
| A | GLN255 |
| A | MET256 |
| A | LEU257 |
| A | ILE260 |
| A | TYR278 |
| A | MET136 |
| A | ARG292 |
| A | GLU295 |
| A | PRO297 |
| A | TFB2002 |
| A | HOH2104 |
| A | HOH2115 |
| A | HOH2128 |
| A | HOH2136 |
| A | HOH2183 |
| A | HOH2210 |
| A | VAL164 |
| A | HOH2350 |
| A | HOH2377 |
| A | HOH2380 |
| A | GLN166 |
| A | ARG187 |
| A | VAL189 |
| A | LYS190 |
| A | GLY191 |
| A | ALA192 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE TFB A 2002 |
| Chain | Residue |
| A | LYS98 |
| A | ASP135 |
| A | TYR278 |
| A | TYR288 |
| A | ARG291 |
| A | ARG292 |
| A | FAD2001 |
| A | HOH2147 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 2003 |
| Chain | Residue |
| A | TYR94 |
| A | TYR224 |
| A | GLU253 |
| A | ARG276 |
| A | HOH2295 |
| A | HOH2310 |
| A | HOH2362 |
| site_id | AC4 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE FAD C 2001 |
| Chain | Residue |
| C | ASP135 |
| C | MET136 |
| C | VAL164 |
| C | GLN166 |
| C | ARG187 |
| C | VAL189 |
| C | LYS190 |
| C | GLY191 |
| C | ALA192 |
| C | TYR193 |
| C | ALA228 |
| C | THR229 |
| C | HIS230 |
| C | ASP231 |
| C | GLN255 |
| C | MET256 |
| C | LEU257 |
| C | ILE260 |
| C | ARG292 |
| C | GLU295 |
| C | PRO297 |
| C | TFB2002 |
| C | HOH2106 |
| C | HOH2110 |
| C | HOH2116 |
| C | HOH2139 |
| C | HOH2190 |
| C | HOH2192 |
| C | HOH2228 |
| C | HOH2263 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE TFB C 2002 |
| Chain | Residue |
| C | LYS98 |
| C | ASP135 |
| C | TYR278 |
| C | TYR288 |
| C | ARG291 |
| C | ARG292 |
| C | FAD2001 |
| C | HOH2160 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:Q72IB8 |
| Chain | Residue | Details |
| A | ASP135 | |
| A | ARG187 | |
| C | ASP135 | |
| C | ARG187 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23151026, ECO:0007744|PDB:4H6Q |
| Chain | Residue | Details |
| A | LYS98 | |
| C | GLN166 | |
| C | ARG187 | |
| C | THR229 | |
| C | ARG291 | |
| C | ARG292 | |
| A | MET136 | |
| A | GLN166 | |
| A | ARG187 | |
| A | THR229 | |
| A | ARG291 | |
| A | ARG292 | |
| C | LYS98 | |
| C | MET136 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | SITE: Critical for catalytic activity => ECO:0000250|UniProtKB:Q72IB8 |
| Chain | Residue | Details |
| A | TYR278 | |
| C | TYR278 |
