5JRH
Crystal structure of Salmonella enterica acetyl-CoA synthetase (Acs) in complex with cAMP and Coenzyme A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003987 | molecular_function | acetate-CoA ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006085 | biological_process | acetyl-CoA biosynthetic process |
| A | 0006935 | biological_process | chemotaxis |
| A | 0016208 | molecular_function | AMP binding |
| A | 0016874 | molecular_function | ligase activity |
| A | 0019427 | biological_process | acetyl-CoA biosynthetic process from acetate |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003987 | molecular_function | acetate-CoA ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006085 | biological_process | acetyl-CoA biosynthetic process |
| B | 0006935 | biological_process | chemotaxis |
| B | 0016208 | molecular_function | AMP binding |
| B | 0016874 | molecular_function | ligase activity |
| B | 0019427 | biological_process | acetyl-CoA biosynthetic process from acetate |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue COA A 701 |
| Chain | Residue |
| A | PHE163 |
| A | HOH802 |
| A | HOH867 |
| A | HOH1031 |
| B | ARG194 |
| A | GLY164 |
| A | GLY165 |
| A | ARG191 |
| A | ASP306 |
| A | SER523 |
| A | HIS525 |
| A | ARG584 |
| A | PRO589 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | binding site for residue CMP A 702 |
| Chain | Residue |
| A | GLY387 |
| A | GLU388 |
| A | PRO389 |
| A | ASP411 |
| A | THR412 |
| A | TRP413 |
| A | TRP414 |
| A | GLN415 |
| A | THR416 |
| A | ASP500 |
| A | ILE512 |
| A | ARG515 |
| A | ASN521 |
| A | ARG526 |
| A | HOH851 |
| A | HOH876 |
| A | HOH907 |
| A | HOH990 |
| A | HOH1109 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 703 |
| Chain | Residue |
| A | VAL537 |
| A | HIS539 |
| A | ILE542 |
| A | HOH1008 |
| A | HOH1141 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue BU3 A 704 |
| Chain | Residue |
| A | GLY173 |
| A | ARG174 |
| A | LYS270 |
| A | PRO271 |
| A | HOH912 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue BU3 A 705 |
| Chain | Residue |
| A | TRP97 |
| A | LYS106 |
| A | PRO143 |
| A | GLU144 |
| A | LEU220 |
| A | LYS221 |
| A | HOH881 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | binding site for residue COA B 701 |
| Chain | Residue |
| A | ARG194 |
| B | PHE163 |
| B | GLY164 |
| B | GLY165 |
| B | ARG191 |
| B | ILE196 |
| B | ASP306 |
| B | ASN335 |
| B | PRO589 |
| B | HOH816 |
| B | HOH847 |
| B | HOH1019 |
| B | HOH1203 |
| site_id | AC7 |
| Number of Residues | 18 |
| Details | binding site for residue CMP B 702 |
| Chain | Residue |
| B | GLY387 |
| B | GLU388 |
| B | PRO389 |
| B | ASP411 |
| B | THR412 |
| B | TRP413 |
| B | TRP414 |
| B | GLN415 |
| B | THR416 |
| B | ASP500 |
| B | ILE512 |
| B | ARG515 |
| B | ASN521 |
| B | ARG526 |
| B | HOH883 |
| B | HOH905 |
| B | HOH948 |
| B | HOH1077 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 703 |
| Chain | Residue |
| B | VAL537 |
| B | HIS539 |
| B | ILE542 |
| B | HOH1142 |
| B | HOH1225 |
| B | HOH1261 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue BU3 B 704 |
| Chain | Residue |
| B | GLY173 |
| B | ASP177 |
| B | TYR263 |
| B | LYS270 |
| B | PRO271 |
| B | HOH999 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue BU3 B 705 |
| Chain | Residue |
| B | TRP97 |
| B | LYS106 |
| B | PRO143 |
| B | GLU144 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 32 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01123","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12627952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17497934","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Hinge residue important for conformational flexibility"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine; by Pat","evidences":[{"source":"HAMAP-Rule","id":"MF_01123","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12493915","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15236963","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
