7KQ6
Crystal Structure of Acetyl-coenzyme A synthetase from Coccidioides immitis in complex with PRX
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 | 0016208 | molecular_function | AMP binding |
A | 0016874 | molecular_function | ligase activity |
A | 0019427 | biological_process | acetyl-CoA biosynthetic process from acetate |
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 | 0016208 | molecular_function | AMP binding |
B | 0016874 | molecular_function | ligase activity |
B | 0019427 | biological_process | acetyl-CoA biosynthetic process from acetate |
C | 0003987 | molecular_function | acetate-CoA ligase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005829 | cellular_component | cytosol |
C | 0006085 | biological_process | acetyl-CoA biosynthetic process |
C | 0016208 | molecular_function | AMP binding |
C | 0016874 | molecular_function | ligase activity |
C | 0019427 | biological_process | acetyl-CoA biosynthetic process from acetate |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 20 |
Details | binding site for residue PRX A 701 |
Chain | Residue |
A | THR328 |
A | GLN431 |
A | THR432 |
A | ASP518 |
A | ILE530 |
A | ARG533 |
A | ASN539 |
A | ARG544 |
A | HOH883 |
A | HOH923 |
A | HOH1081 |
A | VAL402 |
A | HOH1199 |
A | GLY403 |
A | GLU404 |
A | PRO405 |
A | ASP427 |
A | THR428 |
A | TYR429 |
A | TRP430 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue EDO A 702 |
Chain | Residue |
A | TYR29 |
A | SER39 |
A | HOH928 |
A | HOH979 |
A | HOH1070 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue EDO A 703 |
Chain | Residue |
A | LEU47 |
A | ARG61 |
A | ASP65 |
A | TYR308 |
A | HOH804 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue EDO A 704 |
Chain | Residue |
A | ARG103 |
A | LEU339 |
A | LEU340 |
A | HOH1030 |
A | HOH1051 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue EDO A 705 |
Chain | Residue |
A | HIS104 |
A | LYS111 |
A | GLY341 |
A | HOH899 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue EDO A 706 |
Chain | Residue |
A | ARG125 |
A | GLU135 |
A | HOH801 |
A | HOH900 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue EDO A 707 |
Chain | Residue |
A | TYR116 |
A | ARG125 |
A | ILE161 |
A | PRO162 |
A | GLU163 |
A | ARG239 |
A | HOH1216 |
site_id | AC8 |
Number of Residues | 7 |
Details | binding site for residue EDO A 708 |
Chain | Residue |
A | TRP496 |
A | GLY497 |
A | HOH812 |
A | HOH875 |
A | HOH1033 |
B | TRP141 |
B | TYR261 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue EDO A 709 |
Chain | Residue |
A | GLY249 |
A | LEU252 |
A | HOH830 |
A | HOH912 |
A | HOH1230 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue EDO A 710 |
Chain | Residue |
A | LYS71 |
A | ASP74 |
site_id | AD2 |
Number of Residues | 19 |
Details | binding site for residue PRX B 701 |
Chain | Residue |
B | THR328 |
B | VAL402 |
B | GLY403 |
B | GLU404 |
B | PRO405 |
B | ASP427 |
B | THR428 |
B | TYR429 |
B | TRP430 |
B | GLN431 |
B | THR432 |
B | ASP518 |
B | ILE530 |
B | ARG533 |
B | ARG544 |
B | HOH810 |
B | HOH968 |
B | HOH1032 |
B | HOH1071 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue EDO B 702 |
Chain | Residue |
B | TYR29 |
B | SER39 |
B | HOH994 |
B | HOH1063 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue EDO B 703 |
Chain | Residue |
B | LEU47 |
B | ARG61 |
B | ASP65 |
B | TYR308 |
B | HOH806 |
site_id | AD5 |
Number of Residues | 4 |
Details | binding site for residue EDO B 704 |
Chain | Residue |
B | HIS104 |
B | LYS111 |
B | GLY341 |
B | HOH1009 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue EDO B 705 |
Chain | Residue |
B | GLU163 |
B | ARG239 |
B | TYR116 |
B | ARG125 |
B | ILE161 |
site_id | AD7 |
Number of Residues | 6 |
Details | binding site for residue EDO B 706 |
Chain | Residue |
B | GLU117 |
B | PRO121 |
B | GLY122 |
B | ARG358 |
B | LYS365 |
B | HOH1013 |
site_id | AD8 |
Number of Residues | 6 |
Details | binding site for residue EDO B 707 |
Chain | Residue |
B | ARG125 |
B | GLU135 |
B | PHE166 |
B | HOH817 |
B | HOH854 |
B | HOH1186 |
site_id | AD9 |
Number of Residues | 6 |
Details | binding site for residue EDO B 708 |
Chain | Residue |
B | GLY151 |
B | ASP152 |
B | THR153 |
B | ALA197 |
B | ARG198 |
B | HOH895 |
site_id | AE1 |
Number of Residues | 7 |
Details | binding site for residue EDO B 709 |
Chain | Residue |
B | TRP496 |
B | GLY497 |
B | HOH829 |
B | HOH905 |
C | TRP141 |
C | TYR261 |
C | HOH993 |
site_id | AE2 |
Number of Residues | 4 |
Details | binding site for residue EDO B 710 |
Chain | Residue |
B | ASP222 |
B | THR247 |
B | ARG250 |
B | HOH1017 |
site_id | AE3 |
Number of Residues | 4 |
Details | binding site for residue EDO B 711 |
Chain | Residue |
B | ASP243 |
B | VAL244 |
B | TRP253 |
B | HOH1152 |
site_id | AE4 |
Number of Residues | 4 |
Details | binding site for residue EDO B 712 |
Chain | Residue |
B | ASP56 |
B | ARG64 |
B | LYS75 |
B | THR76 |
site_id | AE5 |
Number of Residues | 3 |
Details | binding site for residue EDO B 713 |
Chain | Residue |
B | LYS71 |
B | ASP74 |
C | GLU70 |
site_id | AE6 |
Number of Residues | 5 |
Details | binding site for residue EDO B 714 |
Chain | Residue |
B | ASP85 |
B | HOH963 |
C | ALA130 |
C | GLU131 |
C | LYS134 |
site_id | AE7 |
Number of Residues | 4 |
Details | binding site for residue EDO C 701 |
Chain | Residue |
A | GLU70 |
A | PHE98 |
C | LYS71 |
C | ASP74 |
site_id | AE8 |
Number of Residues | 19 |
Details | binding site for residue PRX C 702 |
Chain | Residue |
C | THR328 |
C | VAL402 |
C | GLY403 |
C | GLU404 |
C | PRO405 |
C | ASP427 |
C | THR428 |
C | TYR429 |
C | TRP430 |
C | GLN431 |
C | THR432 |
C | ASP518 |
C | ILE530 |
C | ARG533 |
C | ARG544 |
C | HOH911 |
C | HOH996 |
C | HOH1029 |
C | HOH1044 |
site_id | AE9 |
Number of Residues | 5 |
Details | binding site for residue EDO C 703 |
Chain | Residue |
C | TYR29 |
C | SER39 |
C | HOH827 |
C | HOH897 |
C | HOH974 |
site_id | AF1 |
Number of Residues | 6 |
Details | binding site for residue EDO C 704 |
Chain | Residue |
C | LEU47 |
C | ARG61 |
C | MET62 |
C | ASP65 |
C | TYR308 |
C | HOH841 |
site_id | AF2 |
Number of Residues | 5 |
Details | binding site for residue EDO C 705 |
Chain | Residue |
C | HIS104 |
C | LYS111 |
C | GLY341 |
C | HOH986 |
C | HOH1158 |
site_id | AF3 |
Number of Residues | 5 |
Details | binding site for residue EDO C 706 |
Chain | Residue |
C | TYR116 |
C | ARG125 |
C | GLU163 |
C | PHE237 |
C | ARG239 |
site_id | AF4 |
Number of Residues | 6 |
Details | binding site for residue EDO C 707 |
Chain | Residue |
C | ARG125 |
C | GLU135 |
C | EDO708 |
C | HOH816 |
C | HOH884 |
C | HOH1162 |
site_id | AF5 |
Number of Residues | 8 |
Details | binding site for residue EDO C 708 |
Chain | Residue |
C | GLU135 |
C | ARG138 |
C | GLU163 |
C | PHE237 |
C | TRP254 |
C | EDO707 |
C | HOH816 |
C | HOH1154 |
site_id | AF6 |
Number of Residues | 4 |
Details | binding site for residue EDO C 709 |
Chain | Residue |
C | ASP222 |
C | THR247 |
C | ARG250 |
C | HOH1089 |
site_id | AF7 |
Number of Residues | 7 |
Details | binding site for residue EDO C 710 |
Chain | Residue |
A | TRP141 |
A | TYR261 |
A | HOH958 |
C | TRP496 |
C | GLY497 |
C | HOH834 |
C | HOH838 |
site_id | AF8 |
Number of Residues | 3 |
Details | binding site for residue EDO C 711 |
Chain | Residue |
C | ASP243 |
C | VAL244 |
C | HOH806 |
Functional Information from PROSITE/UniProt
site_id | PS00455 |
Number of Residues | 12 |
Details | AMP_BINDING Putative AMP-binding domain signature. LLYTSGSTGkPK |
Chain | Residue | Details |
A | LEU278-LYS289 |