5MSW
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 | 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 | 15 |
| Details | binding site for residue AMP A 1201 |
| Chain | Residue |
| A | THR265 |
| A | THR434 |
| A | GLU435 |
| A | ASP507 |
| A | TYR519 |
| A | ARG522 |
| A | LYS629 |
| A | HIS315 |
| A | SER408 |
| A | ALA409 |
| A | PRO410 |
| A | ASP429 |
| A | GLY430 |
| A | TYR431 |
| A | GLY432 |
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: BINDING => ECO:0000255|HAMAP-Rule:MF_02247, ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MST |
| Chain | Residue | Details |
| A | HIS315 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| 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 | ASP429 | |
| A | THR434 | |
| A | ASP507 | |
| A | SER408 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| 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 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02247, ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MSS |
| Chain | Residue | Details |
| A | LYS528 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| 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 | ASP868 | |
| A | SER894 | |
| A | SER934 | |
| A | TYR970 | |
| A | SER997 | |
| A | ARG828 | |
| A | ARG838 | |
| A | ASN801 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| 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 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| 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 |
