5MST
Structure of the A domain of carboxylic acid reductase (CAR) from Segniliparus rugosus in complex with AMP and a co-purified carboxylic acid
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 | 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 | 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 1201 |
| Chain | Residue |
| A | TYR203 |
| A | ASP234 |
| A | HOH1585 |
| A | HOH1741 |
| A | HOH1887 |
| A | HOH1908 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 1202 |
| Chain | Residue |
| A | HOH1802 |
| A | HOH1880 |
| A | HOH1925 |
| A | ALA494 |
| A | PHE497 |
| A | HOH1568 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue FUM A 1203 |
| Chain | Residue |
| A | TRP290 |
| A | PHE294 |
| A | HIS315 |
| A | VAL316 |
| A | SER408 |
| A | GLY430 |
| A | GLY432 |
| A | SER433 |
| A | THR434 |
| A | PRO438 |
| A | AMP1204 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | binding site for residue AMP A 1204 |
| Chain | Residue |
| A | HIS315 |
| A | SER408 |
| A | ALA409 |
| A | PRO410 |
| A | ASP429 |
| A | GLY430 |
| A | TYR431 |
| A | GLY432 |
| A | THR434 |
| A | ASP507 |
| A | TYR519 |
| A | ARG522 |
| A | LYS629 |
| A | FUM1203 |
| A | HOH1393 |
| A | HOH1435 |
| A | HOH1506 |
| A | HOH1526 |
| A | HOH1852 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue CA B 1201 |
| Chain | Residue |
| B | ALA494 |
| B | PHE497 |
| B | HOH1529 |
| B | HOH1848 |
| B | HOH1931 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 1202 |
| Chain | Residue |
| B | TYR203 |
| B | ASP234 |
| B | HOH1541 |
| B | HOH1570 |
| B | HOH1879 |
| B | HOH1937 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | binding site for residue FUM B 1203 |
| Chain | Residue |
| B | TRP290 |
| B | HIS315 |
| B | VAL316 |
| B | SER408 |
| B | GLY430 |
| B | TYR431 |
| B | GLY432 |
| B | SER433 |
| B | LYS629 |
| B | AMP1204 |
| site_id | AC8 |
| Number of Residues | 20 |
| Details | binding site for residue AMP B 1204 |
| Chain | Residue |
| B | HIS315 |
| B | SER408 |
| B | ALA409 |
| B | PRO410 |
| B | ASP429 |
| B | GLY430 |
| B | TYR431 |
| B | GLY432 |
| B | SER433 |
| B | THR434 |
| B | ASP507 |
| B | TYR519 |
| B | ARG522 |
| B | LYS629 |
| B | FUM1203 |
| B | HOH1350 |
| B | HOH1432 |
| B | HOH1540 |
| B | HOH1675 |
| B | HOH1802 |
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 | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02247, ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MST |
| Chain | Residue | Details |
| A | HIS315 | |
| B | HIS315 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02247, ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MSS, ECO:0007744|PDB:5MST, ECO:0007744|PDB:5MSW |
| Chain | Residue | Details |
| A | THR434 | |
| A | ASP507 | |
| B | SER408 | |
| B | ASP429 | |
| B | THR434 | |
| B | ASP507 | |
| A | SER408 | |
| A | ASP429 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02247, ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MST, ECO:0007744|PDB:5MSW |
| Chain | Residue | Details |
| A | TYR519 | |
| A | LYS629 | |
| B | TYR519 | |
| B | LYS629 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02247, ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MSS |
| Chain | Residue | Details |
| A | LYS528 | |
| B | LYS528 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02247, ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MSP, ECO:0007744|PDB:5MSR, ECO:0007744|PDB:5MSV |
| Chain | Residue | Details |
| A | TYR970 | |
| A | SER997 | |
| B | ASN801 | |
| B | ARG828 | |
| B | ARG838 | |
| B | ASP868 | |
| B | SER894 | |
| B | SER934 | |
| B | TYR970 | |
| B | SER997 | |
| A | ARG838 | |
| A | ASP868 | |
| A | SER894 | |
| A | SER934 | |
| A | ASN801 | |
| A | ARG828 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02247, ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MSR, ECO:0007744|PDB:5MSV |
| Chain | Residue | Details |
| A | LYS974 | |
| B | LYS974 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: O-(pantetheine 4'-phosphoryl)serine => ECO:0000255|HAMAP-Rule:MF_02247, ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MSV |
| Chain | Residue | Details |
| A | SER702 | |
| B | SER702 |
