5MSU
Structure of the R domain of carboxylic acid reductase (CAR) from Mycobacterium marinum in complex with NADP, P21 form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001676 | biological_process | long-chain fatty acid metabolic process |
| A | 0004467 | molecular_function | long-chain fatty acid-CoA ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| A | 0031177 | molecular_function | phosphopantetheine binding |
| A | 0050661 | molecular_function | NADP binding |
| B | 0001676 | biological_process | long-chain fatty acid metabolic process |
| B | 0004467 | molecular_function | long-chain fatty acid-CoA ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| B | 0031177 | molecular_function | phosphopantetheine binding |
| B | 0050661 | molecular_function | NADP binding |
| C | 0001676 | biological_process | long-chain fatty acid metabolic process |
| C | 0004467 | molecular_function | long-chain fatty acid-CoA ligase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0006631 | biological_process | fatty acid metabolic process |
| C | 0016020 | cellular_component | membrane |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| C | 0031177 | molecular_function | phosphopantetheine binding |
| C | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 36 |
| Details | binding site for residue NAP C 1201 |
| Chain | Residue |
| A | LYS816 |
| C | LYS855 |
| C | PRO880 |
| C | ALA881 |
| C | ALA882 |
| C | VAL884 |
| C | THR919 |
| C | SER920 |
| C | TYR956 |
| C | LYS960 |
| C | CYS983 |
| C | GLY785 |
| C | ASP984 |
| C | ILE986 |
| C | ASN997 |
| C | HOH1331 |
| C | HOH1353 |
| C | HOH1363 |
| C | HOH1369 |
| C | HOH1378 |
| C | HOH1380 |
| C | HOH1421 |
| C | THR787 |
| C | HOH1427 |
| C | HOH1453 |
| C | HOH1485 |
| C | HOH1510 |
| C | HOH1513 |
| C | HOH1520 |
| C | HOH1552 |
| C | GLY788 |
| C | PHE789 |
| C | LEU790 |
| C | ARG814 |
| C | ARG824 |
| C | ASP854 |
| site_id | AC2 |
| Number of Residues | 34 |
| Details | binding site for residue NAP A 1601 |
| Chain | Residue |
| A | GLY785 |
| A | THR787 |
| A | GLY788 |
| A | PHE789 |
| A | LEU790 |
| A | ARG814 |
| A | ARG824 |
| A | ASP854 |
| A | LYS855 |
| A | PRO880 |
| A | ALA881 |
| A | ALA882 |
| A | VAL884 |
| A | THR919 |
| A | SER920 |
| A | TYR956 |
| A | LYS960 |
| A | CYS983 |
| A | ASP984 |
| A | MET985 |
| A | ILE986 |
| A | ASN997 |
| A | HOH1720 |
| A | HOH1740 |
| A | HOH1760 |
| A | HOH1774 |
| A | HOH1776 |
| A | HOH1785 |
| A | HOH1786 |
| A | HOH1789 |
| A | HOH1825 |
| A | HOH1857 |
| A | HOH1869 |
| A | HOH1898 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | binding site for residue NAP B 1201 |
| Chain | Residue |
| B | GLY785 |
| B | THR787 |
| B | GLY788 |
| B | PHE789 |
| B | LEU790 |
| B | GLY791 |
| B | ARG814 |
| B | ARG824 |
| B | ASP854 |
| B | LYS855 |
| B | PRO880 |
| B | ALA881 |
| B | ALA882 |
| B | THR919 |
| B | TYR956 |
| B | LYS960 |
| B | HOH1394 |
| B | HOH1462 |
| B | HOH1466 |
| B | HOH1491 |
| B | HOH1499 |
| B | HOH1506 |
| B | HOH1554 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SatravddsyAngYSNSKWAGeVLLrEAH |
| Chain | Residue | Details |
| C | SER943-HIS971 |
| site_id | PS00455 |
| Number of Residues | 12 |
| Details | AMP_BINDING Putative AMP-binding domain signature. LIYTSGSTGaPK |
| Chain | Residue | Details |
| C | LEU250-LYS261 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02247 |
| Chain | Residue | Details |
| C | LYS512 | |
| C | LYS612 | |
| A | HIS297 | |
| A | SER392 | |
| A | GLU413 | |
| A | THR418 | |
| A | ASP491 | |
| A | TYR503 | |
| A | LYS512 | |
| A | LYS612 | |
| B | HIS297 | |
| B | SER392 | |
| B | GLU413 | |
| B | THR418 | |
| B | ASP491 | |
| B | TYR503 | |
| B | LYS512 | |
| B | LYS612 | |
| C | SER392 | |
| C | GLU413 | |
| C | THR418 | |
| C | ASP491 | |
| C | TYR503 | |
| C | HIS297 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MSO, ECO:0007744|PDB:5MSU |
| Chain | Residue | Details |
| C | THR787 | |
| C | THR919 | |
| A | THR787 | |
| A | THR919 | |
| B | THR787 | |
| B | THR919 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02247, ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MSO, ECO:0007744|PDB:5MSU |
| Chain | Residue | Details |
| A | ARG814 | |
| A | ARG824 | |
| A | ASP854 | |
| A | PRO880 | |
| A | TYR956 | |
| A | LYS960 | |
| B | ARG814 | |
| B | ARG824 | |
| B | ASP854 | |
| B | PRO880 | |
| B | TYR956 | |
| B | LYS960 | |
| C | ARG814 | |
| C | ARG824 | |
| C | ASP854 | |
| C | PRO880 | |
| C | TYR956 | |
| C | LYS960 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | MOD_RES: O-(pantetheine 4'-phosphoryl)serine => ECO:0000255|HAMAP-Rule:MF_02247 |
| Chain | Residue | Details |
| C | SER685 | |
| A | SER685 | |
| B | SER685 |
