5MSS
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 | 17 |
Details | binding site for residue AMP A 1201 |
Chain | Residue |
A | VAL316 |
A | THR434 |
A | ASP507 |
A | TYR519 |
A | LYS528 |
A | PHE534 |
A | HOH1307 |
A | HOH1415 |
A | HOH1482 |
A | SER408 |
A | ALA409 |
A | PRO410 |
A | ASP429 |
A | GLY430 |
A | TYR431 |
A | GLY432 |
A | SER433 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue NA A 1202 |
Chain | Residue |
A | LEU529 |
A | GLN531 |
A | GLY532 |
A | GLU533 |
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 | LYS629 | |
A | TYR519 |
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 | ASN801 | |
A | ARG828 | |
A | ARG838 |
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 |