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 |