5MSV
Structure of the phosphopantetheine modified PCP-R didomain of carboxylic acid reductase (CAR) in complex with NADP
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 |
| C | 0001676 | biological_process | long-chain fatty acid metabolic process |
| C | 0004467 | molecular_function | long-chain fatty acid-CoA ligase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0016020 | cellular_component | membrane |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| C | 0031177 | molecular_function | phosphopantetheine binding |
| C | 0050661 | molecular_function | NADP binding |
| D | 0001676 | biological_process | long-chain fatty acid metabolic process |
| D | 0004467 | molecular_function | long-chain fatty acid-CoA ligase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006629 | biological_process | lipid metabolic process |
| D | 0016020 | cellular_component | membrane |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| D | 0031177 | molecular_function | phosphopantetheine binding |
| D | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue PNS A 1201 |
| Chain | Residue |
| A | ASP701 |
| A | GLN1015 |
| A | ARG1018 |
| A | HOH1336 |
| A | HOH1356 |
| A | HOH1459 |
| A | SER702 |
| A | VAL898 |
| A | ASN899 |
| A | HIS900 |
| A | VAL901 |
| A | TYR970 |
| A | PRO1013 |
| A | ASP1014 |
| site_id | AC2 |
| Number of Residues | 32 |
| Details | binding site for residue NAP A 1202 |
| Chain | Residue |
| A | GLY799 |
| A | ASN801 |
| A | GLY802 |
| A | TRP803 |
| A | LEU804 |
| A | ARG828 |
| A | ARG838 |
| A | ASP868 |
| A | PHE869 |
| A | SER894 |
| A | GLY895 |
| A | ALA896 |
| A | VAL898 |
| A | LEU933 |
| A | SER934 |
| A | TYR970 |
| A | LYS974 |
| A | SER997 |
| A | ASN1011 |
| A | HOH1321 |
| A | HOH1336 |
| A | HOH1339 |
| A | HOH1345 |
| A | HOH1358 |
| A | HOH1388 |
| A | HOH1396 |
| A | HOH1408 |
| A | HOH1421 |
| A | HOH1438 |
| A | HOH1442 |
| A | HOH1449 |
| A | HOH1451 |
| site_id | AC3 |
| Number of Residues | 32 |
| Details | binding site for residue NAP B 1202 |
| Chain | Residue |
| B | GLY799 |
| B | ASN801 |
| B | GLY802 |
| B | TRP803 |
| B | LEU804 |
| B | ARG828 |
| B | ARG838 |
| B | ASP868 |
| B | PHE869 |
| B | SER894 |
| B | GLY895 |
| B | ALA896 |
| B | VAL898 |
| B | LEU933 |
| B | SER934 |
| B | TYR970 |
| B | LYS974 |
| B | SER997 |
| B | ASN1011 |
| B | HOH1303 |
| B | HOH1309 |
| B | HOH1316 |
| B | HOH1340 |
| B | HOH1345 |
| B | HOH1350 |
| B | HOH1360 |
| B | HOH1369 |
| B | HOH1375 |
| B | HOH1413 |
| B | HOH1422 |
| B | HOH1448 |
| B | HOH1450 |
| site_id | AC4 |
| Number of Residues | 31 |
| Details | binding site for residue NAP C 1202 |
| Chain | Residue |
| C | HOH1333 |
| C | HOH1335 |
| C | HOH1340 |
| C | HOH1349 |
| C | HOH1368 |
| C | HOH1370 |
| C | HOH1402 |
| C | HOH1406 |
| C | HOH1408 |
| C | HOH1421 |
| C | GLY799 |
| C | ASN801 |
| C | GLY802 |
| C | TRP803 |
| C | LEU804 |
| C | ARG828 |
| C | ARG838 |
| C | ASP868 |
| C | PHE869 |
| C | SER894 |
| C | GLY895 |
| C | ALA896 |
| C | VAL898 |
| C | LEU933 |
| C | SER934 |
| C | TYR970 |
| C | LYS974 |
| C | SER997 |
| C | ASN1011 |
| C | HOH1309 |
| C | HOH1316 |
| site_id | AC5 |
| Number of Residues | 29 |
| Details | binding site for residue NAP D 1202 |
| Chain | Residue |
| D | GLY799 |
| D | ASN801 |
| D | GLY802 |
| D | TRP803 |
| D | LEU804 |
| D | ARG828 |
| D | ARG838 |
| D | ASP868 |
| D | PHE869 |
| D | SER894 |
| D | GLY895 |
| D | ALA896 |
| D | VAL898 |
| D | LEU933 |
| D | SER934 |
| D | TYR970 |
| D | LYS974 |
| D | SER997 |
| D | ASN1011 |
| D | HOH1310 |
| D | HOH1327 |
| D | HOH1339 |
| D | HOH1345 |
| D | HOH1366 |
| D | HOH1368 |
| D | HOH1387 |
| D | HOH1403 |
| D | HOH1418 |
| D | HOH1446 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | binding site for Di-peptide PNS B 1201 and SER B 702 |
| Chain | Residue |
| B | ASP701 |
| B | LEU703 |
| B | ALA705 |
| B | LEU706 |
| B | ASN899 |
| B | HIS900 |
| B | VAL901 |
| B | TYR970 |
| B | PRO1013 |
| B | ASP1014 |
| B | GLN1015 |
| B | ARG1018 |
| B | HOH1321 |
| B | HOH1340 |
| B | HOH1375 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | binding site for Di-peptide PNS C 1201 and SER C 702 |
| Chain | Residue |
| C | ASP701 |
| C | LEU703 |
| C | ALA705 |
| C | LEU706 |
| C | ASN899 |
| C | HIS900 |
| C | MET999 |
| C | PRO1013 |
| C | ASP1014 |
| C | GLN1015 |
| C | ARG1018 |
| C | HOH1350 |
| C | HOH1408 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | binding site for Di-peptide PNS D 1201 and SER D 702 |
| Chain | Residue |
| D | ASP701 |
| D | LEU703 |
| D | ALA705 |
| D | LEU706 |
| D | VAL898 |
| D | ASN899 |
| D | HIS900 |
| D | MET999 |
| D | PRO1013 |
| D | ASP1014 |
| D | GLN1015 |
| D | ARG1018 |
| D | HOH1380 |
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 | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02247, ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MST |
| Chain | Residue | Details |
| A | HIS315 | |
| B | HIS315 | |
| C | HIS315 | |
| D | HIS315 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| 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 | SER408 | |
| C | ASP429 | |
| C | THR434 | |
| C | ASP507 | |
| D | SER408 | |
| D | ASP429 | |
| D | THR434 | |
| D | ASP507 | |
| A | ASP429 | |
| A | THR434 | |
| A | ASP507 | |
| B | SER408 | |
| B | ASP429 | |
| B | THR434 | |
| B | ASP507 | |
| C | SER408 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| 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 | |
| C | TYR519 | |
| C | LYS629 | |
| D | TYR519 | |
| D | LYS629 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02247, ECO:0000269|PubMed:28719588, ECO:0007744|PDB:5MSS |
| Chain | Residue | Details |
| A | LYS528 | |
| B | LYS528 | |
| C | LYS528 | |
| D | LYS528 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 32 |
| 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 | ASN801 | |
| B | ARG828 | |
| B | ARG838 | |
| B | ASP868 | |
| B | SER894 | |
| B | SER934 | |
| B | TYR970 | |
| B | SER997 | |
| C | ASN801 | |
| C | ARG828 | |
| C | ARG838 | |
| A | ARG828 | |
| C | ASP868 | |
| C | SER894 | |
| C | SER934 | |
| C | TYR970 | |
| C | SER997 | |
| D | ASN801 | |
| D | ARG828 | |
| D | ARG838 | |
| D | ASP868 | |
| D | SER894 | |
| A | ARG838 | |
| D | SER934 | |
| D | TYR970 | |
| D | SER997 | |
| A | ASP868 | |
| A | SER894 | |
| A | SER934 | |
| A | TYR970 | |
| A | SER997 | |
| B | ASN801 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| 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 | |
| C | LYS974 | |
| D | LYS974 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| 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 | |
| C | SER702 | |
| D | SER702 |
