2P2B
Acetyl-CoA Synthetase, V386A mutation
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0016877 | molecular_function | ligase activity, forming carbon-sulfur bonds |
| A | 0019427 | biological_process | acetyl-CoA biosynthetic process from acetate |
| A | 0046872 | molecular_function | metal ion 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 | 0016877 | molecular_function | ligase activity, forming carbon-sulfur bonds |
| 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 | 17 |
| Details | BINDING SITE FOR RESIDUE COA A 990 |
| Chain | Residue |
| A | PHE163 |
| A | ALA360 |
| A | ALA363 |
| A | SER523 |
| A | HIS525 |
| A | ARG584 |
| A | PRO589 |
| A | HOH1139 |
| A | HOH1140 |
| A | GLY164 |
| A | GLY165 |
| A | ARG191 |
| A | ARG194 |
| A | ILE196 |
| A | VAL333 |
| A | PRO334 |
| A | ASN335 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE COA B 991 |
| Chain | Residue |
| B | PHE163 |
| B | GLY164 |
| B | GLY165 |
| B | ARG191 |
| B | ALA192 |
| B | ARG194 |
| B | ILE196 |
| B | VAL333 |
| B | PRO334 |
| B | ASN335 |
| B | TRP336 |
| B | SER523 |
| B | ARG584 |
| B | PRO589 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PRX A 999 |
| Chain | Residue |
| A | VAL310 |
| A | THR311 |
| A | GLY387 |
| A | GLU388 |
| A | PRO389 |
| A | ASP411 |
| A | THR412 |
| A | TRP413 |
| A | TRP414 |
| A | GLN415 |
| A | THR416 |
| A | ASP500 |
| A | ARG515 |
| A | ARG526 |
| A | HOH1155 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PRX B 998 |
| Chain | Residue |
| B | THR311 |
| B | GLY387 |
| B | GLU388 |
| B | PRO389 |
| B | ASP411 |
| B | THR412 |
| B | TRP413 |
| B | TRP414 |
| B | GLN415 |
| B | THR416 |
| B | ASP500 |
| B | ARG515 |
| B | ARG526 |
| B | HOH1070 |
| B | HOH1110 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 18 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ARG191 | |
| B | ARG191 | |
| B | GLY387 | |
| B | ASP411 | |
| B | ASP500 | |
| B | ARG515 | |
| B | ARG526 | |
| B | VAL537 | |
| B | HIS539 | |
| B | ILE542 | |
| A | GLY387 | |
| A | ASP411 | |
| A | ASP500 | |
| A | ARG515 | |
| A | ARG526 | |
| A | VAL537 | |
| A | HIS539 | |
| A | ILE542 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01123, ECO:0000269|PubMed:12627952, ECO:0000269|PubMed:17497934 |
| Chain | Residue | Details |
| A | THR311 | |
| A | ASN335 | |
| A | SER523 | |
| A | ARG584 | |
| B | THR311 | |
| B | ASN335 | |
| B | SER523 | |
| B | ARG584 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | SITE: Hinge residue important for conformational flexibility |
| Chain | Residue | Details |
| A | ASP517 | |
| B | ASP517 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine; by Pat => ECO:0000255|HAMAP-Rule:MF_01123, ECO:0000269|PubMed:12493915, ECO:0000269|PubMed:15236963 |
| Chain | Residue | Details |
| A | LYS609 | |
| B | LYS609 |
