5MSP
Structure of the unmodified PCP-R didomain of carboxylic acid reductase (CAR) from Segniliparus rugosus in complex with NADP, F2221 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 | 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 | 23 |
Details | binding site for residue NAP A 1201 |
Chain | Residue |
A | GLY799 |
A | SER894 |
A | GLY895 |
A | ALA896 |
A | VAL898 |
A | LEU933 |
A | SER934 |
A | TYR970 |
A | LYS974 |
A | SER997 |
A | HOH1305 |
A | ASN801 |
A | HOH1307 |
A | HOH1317 |
A | HOH1322 |
A | HOH1330 |
A | GLY802 |
A | TRP803 |
A | LEU804 |
A | ARG828 |
A | ARG838 |
A | ASP868 |
A | PHE869 |
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 |