6X3B
Structure of RMD from Pseudomonas aeruginosa complexed with NADPH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| A | 0009243 | biological_process | O antigen biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019306 | biological_process | GDP-D-rhamnose biosynthetic process |
| A | 0033705 | molecular_function | GDP-4-dehydro-6-deoxy-D-mannose reductase activity |
| A | 0070402 | molecular_function | NADPH binding |
| B | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| B | 0009243 | biological_process | O antigen biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019306 | biological_process | GDP-D-rhamnose biosynthetic process |
| B | 0033705 | molecular_function | GDP-4-dehydro-6-deoxy-D-mannose reductase activity |
| B | 0070402 | molecular_function | NADPH binding |
| C | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| C | 0009243 | biological_process | O antigen biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0019306 | biological_process | GDP-D-rhamnose biosynthetic process |
| C | 0033705 | molecular_function | GDP-4-dehydro-6-deoxy-D-mannose reductase activity |
| C | 0070402 | molecular_function | NADPH binding |
| D | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| D | 0009243 | biological_process | O antigen biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0019306 | biological_process | GDP-D-rhamnose biosynthetic process |
| D | 0033705 | molecular_function | GDP-4-dehydro-6-deoxy-D-mannose reductase activity |
| D | 0070402 | molecular_function | NADPH binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| Details | binding site for residue NDP A 401 |
| Chain | Residue |
| A | GLY9 |
| A | ALA61 |
| A | GLY62 |
| A | THR64 |
| A | ILE103 |
| A | SER104 |
| A | TYR131 |
| A | LYS135 |
| A | HIS161 |
| A | GLN166 |
| A | PHE170 |
| A | SER11 |
| A | HOH501 |
| A | HOH508 |
| A | HOH509 |
| A | HOH517 |
| A | HOH528 |
| A | HOH537 |
| A | HOH543 |
| A | HOH545 |
| A | HOH546 |
| A | HOH608 |
| A | GLY12 |
| A | HOH623 |
| A | HOH625 |
| B | ARG265 |
| A | PHE13 |
| A | VAL14 |
| A | TYR38 |
| A | ASP39 |
| A | LEU40 |
| A | LEU60 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue NO3 A 402 |
| Chain | Residue |
| A | GLY106 |
| A | ASP107 |
| A | GLY110 |
| A | HOH601 |
| site_id | AC3 |
| Number of Residues | 32 |
| Details | binding site for residue NDP B 401 |
| Chain | Residue |
| B | GLY9 |
| B | SER11 |
| B | GLY12 |
| B | PHE13 |
| B | VAL14 |
| B | ASP39 |
| B | LEU40 |
| B | LEU60 |
| B | ALA61 |
| B | GLY62 |
| B | THR64 |
| B | ILE103 |
| B | SER104 |
| B | SER105 |
| B | TYR131 |
| B | LYS135 |
| B | PRO158 |
| B | HIS161 |
| B | GLN166 |
| B | PHE170 |
| B | HOH519 |
| B | HOH527 |
| B | HOH531 |
| B | HOH532 |
| B | HOH537 |
| B | HOH541 |
| B | HOH542 |
| B | HOH547 |
| B | HOH575 |
| B | HOH582 |
| B | HOH593 |
| B | HOH620 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue POP B 402 |
| Chain | Residue |
| B | ASP107 |
| B | ASN129 |
| B | ARG200 |
| B | HOH520 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | binding site for residue NDP C 401 |
| Chain | Residue |
| C | GLY9 |
| C | SER11 |
| C | GLY12 |
| C | PHE13 |
| C | VAL14 |
| C | ASP39 |
| C | LEU40 |
| C | LEU60 |
| C | ALA61 |
| C | GLY62 |
| C | THR64 |
| C | ILE103 |
| C | TYR131 |
| C | LYS135 |
| C | PRO158 |
| C | HIS161 |
| C | GLN166 |
| C | PHE170 |
| C | HOH501 |
| C | HOH505 |
| C | HOH525 |
| C | HOH531 |
| C | HOH539 |
| C | HOH556 |
| C | HOH558 |
| site_id | AC6 |
| Number of Residues | 24 |
| Details | binding site for residue NDP D 401 |
| Chain | Residue |
| D | GLY12 |
| D | PHE13 |
| D | VAL14 |
| D | ARG37 |
| D | ASP39 |
| D | LEU40 |
| D | LEU60 |
| D | ALA61 |
| D | GLY62 |
| D | THR64 |
| D | ILE103 |
| D | SER104 |
| D | TYR131 |
| D | LYS135 |
| D | HIS161 |
| D | GLN166 |
| D | HOH508 |
| D | HOH511 |
| D | HOH514 |
| D | HOH515 |
| D | HOH520 |
| D | HOH544 |
| D | GLY9 |
| D | SER11 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | binding site for residue NDP D 402 |
| Chain | Residue |
| D | VAL66 |
| D | PRO67 |
| D | PHE70 |
| D | ASP107 |
| D | ASN129 |
| D | TYR131 |
| D | PRO158 |
| D | PHE159 |
| D | ASN160 |
| D | ARG200 |
| D | VAL267 |
| D | HOH501 |
| D | HOH522 |
| D | HOH532 |
| D | HOH556 |
| D | HOH565 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. PiheeliphpRnpYAVSKLAAeSLClQWG |
| Chain | Residue | Details |
| A | PRO118-GLY146 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| B | ASP39 | |
| B | SER105 | |
| B | TYR131 | |
| B | ASN160 | |
| B | ARG200 | |
| B | ARG260 | |
| C | PHE13 | |
| C | ASP39 | |
| C | SER105 | |
| C | TYR131 | |
| C | ASN160 | |
| C | ARG200 | |
| C | ARG260 | |
| D | PHE13 | |
| D | ASP39 | |
| D | SER105 | |
| D | TYR131 | |
| D | ASN160 | |
| D | ARG200 | |
| D | ARG260 | |
| A | PHE13 | |
| A | ASP39 | |
| A | SER105 | |
| A | TYR131 | |
| A | ASN160 | |
| A | ARG200 | |
| A | ARG260 | |
| B | PHE13 |
