1XPL
Crystal Structure of Staphylococcus aureus HMG-COA Synthase with Acetoacetyl-COA and Acetylated Cysteine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004421 | molecular_function | hydroxymethylglutaryl-CoA synthase activity |
A | 0006084 | biological_process | acetyl-CoA metabolic process |
A | 0010142 | biological_process | farnesyl diphosphate biosynthetic process, mevalonate pathway |
A | 0016746 | molecular_function | acyltransferase activity |
B | 0004421 | molecular_function | hydroxymethylglutaryl-CoA synthase activity |
B | 0006084 | biological_process | acetyl-CoA metabolic process |
B | 0010142 | biological_process | farnesyl diphosphate biosynthetic process, mevalonate pathway |
B | 0016746 | molecular_function | acyltransferase activity |
C | 0004421 | molecular_function | hydroxymethylglutaryl-CoA synthase activity |
C | 0006084 | biological_process | acetyl-CoA metabolic process |
C | 0010142 | biological_process | farnesyl diphosphate biosynthetic process, mevalonate pathway |
C | 0016746 | molecular_function | acyltransferase activity |
D | 0004421 | molecular_function | hydroxymethylglutaryl-CoA synthase activity |
D | 0006084 | biological_process | acetyl-CoA metabolic process |
D | 0010142 | biological_process | farnesyl diphosphate biosynthetic process, mevalonate pathway |
D | 0016746 | molecular_function | acyltransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 1501 |
Chain | Residue |
A | LYS192 |
A | TYR193 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 1502 |
Chain | Residue |
A | GLY148 |
A | HOH1530 |
site_id | AC3 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE CAA A 1401 |
Chain | Residue |
A | TYR143 |
A | GLY148 |
A | PHE185 |
A | VAL196 |
A | GLY198 |
A | SER201 |
A | TYR205 |
A | HIS233 |
A | PRO235 |
A | PHE236 |
A | MET239 |
A | ASN275 |
A | SER307 |
A | HOH1523 |
A | HOH1588 |
A | HOH1599 |
A | ASP29 |
A | ASN31 |
A | GLY36 |
A | CYS111 |
A | SCY111 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 2501 |
Chain | Residue |
B | HIS191 |
B | LYS192 |
B | TYR193 |
B | HOH2622 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 2502 |
Chain | Residue |
B | SER147 |
B | GLY148 |
B | HOH2536 |
site_id | AC6 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE CAA B 2401 |
Chain | Residue |
B | ASP29 |
B | ASN31 |
B | LYS32 |
B | GLY36 |
B | SCY111 |
B | CYS111 |
B | TYR143 |
B | GLY148 |
B | SER201 |
B | HIS233 |
B | PRO235 |
B | PHE236 |
B | MET239 |
B | ASN275 |
B | SER307 |
B | HOH2529 |
B | HOH2586 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 C 3501 |
Chain | Residue |
C | HIS191 |
C | LYS192 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 C 3502 |
Chain | Residue |
C | SER147 |
C | GLY148 |
C | HOH3532 |
site_id | AC9 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE CAA C 3401 |
Chain | Residue |
C | ASP29 |
C | ASN31 |
C | LYS32 |
C | GLY36 |
C | SCY111 |
C | CYS111 |
C | TYR143 |
C | GLY148 |
C | GLY149 |
C | THR152 |
C | SER201 |
C | HIS233 |
C | PRO235 |
C | PHE236 |
C | LYS238 |
C | ASN275 |
C | SER307 |
C | HOH3561 |
C | HOH3607 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 D 4501 |
Chain | Residue |
D | HIS191 |
D | LYS192 |
D | TYR193 |
site_id | BC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE SO4 D 4502 |
Chain | Residue |
D | GLY148 |
site_id | BC3 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE CAA D 4401 |
Chain | Residue |
D | ASP29 |
D | ASN31 |
D | LYS32 |
D | GLY36 |
D | CYS111 |
D | SCY111 |
D | TYR143 |
D | GLY148 |
D | GLY198 |
D | SER201 |
D | TYR205 |
D | HIS233 |
D | PRO235 |
D | PHE236 |
D | ASN275 |
D | SER307 |
D | HOH4522 |
D | HOH4595 |