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 | 2 |
Details | BINDING SITE FOR RESIDUE CL B 901 |
Chain | Residue |
B | LYS221 |
B | ARG238 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 902 |
Chain | Residue |
A | LYS221 |
A | ARG238 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 903 |
Chain | Residue |
B | HOH2180 |
B | VAL537 |
B | HIS539 |
B | ILE542 |
B | HOH1893 |
B | HOH2179 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 904 |
Chain | Residue |
A | VAL537 |
A | HIS539 |
A | ILE542 |
A | HOH1877 |
A | HOH1910 |
A | HOH2208 |
site_id | AC5 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE COA A 990 |
Chain | Residue |
A | PHE163 |
A | GLY165 |
A | ARG191 |
A | TRP309 |
A | ALA357 |
A | THR359 |
A | VAL386 |
A | SER523 |
A | GLY524 |
A | ARG584 |
A | PRO589 |
A | HOH1854 |
A | HOH1883 |
A | HOH1923 |
A | HOH2133 |
A | HOH2162 |
A | HOH2163 |
site_id | AC6 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE COA B 991 |
Chain | Residue |
B | PHE163 |
B | GLY165 |
B | ARG191 |
B | ILE196 |
B | TRP309 |
B | ALA357 |
B | THR359 |
B | VAL386 |
B | SER523 |
B | GLY524 |
B | ARG584 |
B | PRO589 |
B | HOH1883 |
B | HOH2010 |
B | HOH2014 |
B | HOH2060 |
B | HOH2092 |
B | HOH2093 |
B | HOH2110 |
B | HOH2131 |
site_id | AC7 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE PRX A 999 |
Chain | Residue |
A | THR311 |
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 | ARG526 |
A | HOH1887 |
A | HOH2054 |
A | HOH2056 |
A | HOH2078 |
A | HOH2201 |
site_id | AC8 |
Number of Residues | 19 |
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 | ILE512 |
B | ARG515 |
B | ARG526 |
B | HOH2005 |
B | HOH2023 |
B | HOH2030 |
B | HOH2104 |
B | HOH2111 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO B 1800 |
Chain | Residue |
B | VAL161 |
B | ILE162 |
B | PHE163 |
B | PHE166 |
B | TYR263 |
B | GLY308 |
B | HOH1834 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 1801 |
Chain | Residue |
A | ILE162 |
A | PHE163 |
A | PHE166 |
A | TYR263 |
A | GLY308 |
A | VAL161 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 1802 |
Chain | Residue |
A | GLU41 |
A | GLN42 |
A | ILE45 |
A | HOH1891 |
A | HOH1996 |
site_id | BC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO A 1803 |
Chain | Residue |
A | GLY164 |
A | GLY165 |
A | PHE166 |
A | SER167 |
A | ILE196 |
A | ASN201 |
A | PRO589 |
A | HOH2035 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 1804 |
Chain | Residue |
B | VAL190 |
B | GLY193 |
B | ARG194 |
B | SER195 |
Functional Information from PROSITE/UniProt
site_id | PS00018 |
Number of Residues | 13 |
Details | EF_HAND_1 EF-hand calcium-binding domain. DTSQSKHISyrEL |
Chain | Residue | Details |
A | ASP101-LEU113 | |
site_id | PS00455 |
Number of Residues | 12 |
Details | AMP_BINDING Putative AMP-binding domain signature. ILYTSGSTGkPK |
Chain | Residue | Details |
A | ILE261-LYS272 | |
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 | |
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 | |
Chain | Residue | Details |
A | LYS609 | |
B | LYS609 | |