5ZIX
Crystal structure of Ketopantoate reductase from Pseudomonas aeruginosa bound to NADP+
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008677 | molecular_function | 2-dehydropantoate 2-reductase activity |
| A | 0015940 | biological_process | pantothenate biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0050661 | molecular_function | NADP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008677 | molecular_function | 2-dehydropantoate 2-reductase activity |
| B | 0015940 | biological_process | pantothenate biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0050661 | molecular_function | NADP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008677 | molecular_function | 2-dehydropantoate 2-reductase activity |
| C | 0015940 | biological_process | pantothenate biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 401 |
| Chain | Residue |
| A | GLU49 |
| A | PHE139 |
| A | ALA140 |
| A | ARG142 |
| A | HOH569 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 402 |
| Chain | Residue |
| A | ARG114 |
| C | LEU195 |
| C | ARG290 |
| C | HIS294 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 403 |
| Chain | Residue |
| A | LEU195 |
| A | HIS294 |
| A | GLN297 |
| A | ARG298 |
| A | HOH506 |
| A | HOH532 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | binding site for residue NAP A 404 |
| Chain | Residue |
| A | GLY7 |
| A | ALA8 |
| A | GLY9 |
| A | SER10 |
| A | LEU11 |
| A | ARG31 |
| A | ARG35 |
| A | ALA75 |
| A | CYS76 |
| A | ALA84 |
| A | LEU101 |
| A | GLN102 |
| A | ASN103 |
| A | SER125 |
| A | GLU127 |
| A | GLY128 |
| A | ALA129 |
| A | ARG131 |
| A | GLU262 |
| A | HOH524 |
| A | HOH526 |
| site_id | AC5 |
| Number of Residues | 26 |
| Details | binding site for residue NAP B 401 |
| Chain | Residue |
| B | LEU6 |
| B | GLY7 |
| B | ALA8 |
| B | GLY9 |
| B | SER10 |
| B | LEU11 |
| B | ARG31 |
| B | ARG35 |
| B | ALA75 |
| B | CYS76 |
| B | LYS77 |
| B | ASP80 |
| B | ALA84 |
| B | LEU101 |
| B | GLN102 |
| B | ASN103 |
| B | GLU127 |
| B | GLY128 |
| B | ALA129 |
| B | ARG131 |
| B | GLU262 |
| B | HOH505 |
| B | HOH518 |
| B | HOH525 |
| B | HOH543 |
| B | HOH568 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P0A9J4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 27 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2018","submissionDatabase":"PDB data bank","title":"Crystal structure of Ketopantoate reductase from Pseudomonas aeruginosa bound to NADP+.","authors":["Khanppnavar B.","Datta S."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 15 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P0A9J4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
