5MSS
Structure of the A-PCP didomain of carboxylic acid reductase (CAR) from Segniliparus rugosus in complex with AMP
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 | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | binding site for residue AMP A 1201 |
| Chain | Residue |
| A | VAL316 |
| A | THR434 |
| A | ASP507 |
| A | TYR519 |
| A | LYS528 |
| A | PHE534 |
| A | HOH1307 |
| A | HOH1415 |
| A | HOH1482 |
| A | SER408 |
| A | ALA409 |
| A | PRO410 |
| A | ASP429 |
| A | GLY430 |
| A | TYR431 |
| A | GLY432 |
| A | SER433 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue NA A 1202 |
| Chain | Residue |
| A | LEU529 |
| A | GLN531 |
| A | GLY532 |
| A | GLU533 |
Functional Information from PROSITE/UniProt
| site_id | PS00455 |
| Number of Residues | 12 |
| Details | AMP_BINDING Putative AMP-binding domain signature. LIYTSGSTGtPK |
| Chain | Residue | Details |
| A | LEU262-LYS273 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02247","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"28719588","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5MST","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02247","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"28719588","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5MSS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MST","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MSW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02247","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"28719588","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5MST","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MSW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02247","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"28719588","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5MSS","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"O-(pantetheine 4'-phosphoryl)serine","evidences":[{"source":"HAMAP-Rule","id":"MF_02247","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"28719588","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5MSV","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
