2P2Q
Acetyl-CoA Synthetase, R584E mutation
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 | 15 |
| Details | BINDING SITE FOR RESIDUE PRX A 999 |
| Chain | Residue |
| A | THR311 |
| A | THR416 |
| A | ASP500 |
| A | ILE512 |
| A | ARG515 |
| A | ARG526 |
| A | HOH1110 |
| A | GLY387 |
| A | GLU388 |
| A | PRO389 |
| A | ASP411 |
| A | THR412 |
| A | TRP413 |
| A | TRP414 |
| A | GLN415 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PRX B 998 |
| Chain | Residue |
| B | THR311 |
| B | VAL386 |
| 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 | ARG526 |
| B | HOH1112 |
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 |
