5MSD
Structure of the A domain of carboxylic acid reductase (CAR) from Nocardia iowensis in complex with AMP and benzoic acid
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 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 | 0047683 | molecular_function | aryl-aldehyde dehydrogenase (NADP+) activity |
| A | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | binding site for residue AMP A 1201 |
| Chain | Residue |
| A | THR255 |
| A | THR421 |
| A | ASP495 |
| A | TYR507 |
| A | ARG510 |
| A | LYS616 |
| A | BEZ1202 |
| A | HOH1327 |
| A | HOH1492 |
| A | HOH1506 |
| A | HIS300 |
| A | SER395 |
| A | ALA396 |
| A | PRO397 |
| A | ASP416 |
| A | GLY417 |
| A | TYR418 |
| A | GLY419 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue BEZ A 1202 |
| Chain | Residue |
| A | HIS300 |
| A | ILE301 |
| A | SER395 |
| A | GLY417 |
| A | GLY419 |
| A | SER420 |
| A | ALA425 |
| A | AMP1201 |
| A | HOH1492 |
| A | HOH1776 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SavrvvresyAngYGNSKWAGeVLLrEAH |
| Chain | Residue | Details |
| A | SER943-HIS971 |
| site_id | PS00455 |
| Number of Residues | 12 |
| Details | AMP_BINDING Putative AMP-binding domain signature. LIYTSGSTGtPK |
| Chain | Residue | Details |
| A | LEU252-LYS263 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02247","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"28719588","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5MSC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MSD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MSQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02247","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"28719588","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5MSD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MSQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02247","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
