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 |
A | PHE13 | |
B | SER105 | |
B | TYR131 | |
B | ASN160 | |
B | ARG200 | |
B | ARG260 | |
C | PHE13 | |
C | ASP39 | |
C | SER105 | |
C | TYR131 | |
C | ASN160 | |
A | ASP39 | |
C | ARG200 | |
C | ARG260 | |
D | PHE13 | |
D | ASP39 | |
D | SER105 | |
D | TYR131 | |
D | ASN160 | |
D | ARG200 | |
D | ARG260 | |
A | SER105 | |
A | TYR131 | |
A | ASN160 | |
A | ARG200 | |
A | ARG260 | |
B | PHE13 | |
B | ASP39 |