2CTZ
Crystal structure of o-acetyl homoserine sulfhydrylase from Thermus thermophilus HB8
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0009086 | biological_process | methionine biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| A | 0019346 | biological_process | transsulfuration |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0051009 | molecular_function | O-acetylhomoserine sulfhydrylase activity |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0009086 | biological_process | methionine biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| B | 0019346 | biological_process | transsulfuration |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0051009 | molecular_function | O-acetylhomoserine sulfhydrylase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP A 600 |
| Chain | Residue |
| A | SER81 |
| A | LYS206 |
| A | HOH677 |
| A | HOH679 |
| B | ARG54 |
| A | GLY82 |
| A | HIS83 |
| A | GLN86 |
| A | TYR107 |
| A | ASP180 |
| A | THR182 |
| A | SER203 |
| A | THR205 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP B 600 |
| Chain | Residue |
| A | ARG54 |
| B | SER81 |
| B | GLY82 |
| B | HIS83 |
| B | GLN86 |
| B | TYR107 |
| B | ASP180 |
| B | THR182 |
| B | SER203 |
| B | THR205 |
| B | LYS206 |
| B | HOH686 |
| B | HOH687 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|Ref.3 |
| Chain | Residue | Details |
| A | LYS206 | |
| B | LYS206 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| A | TYR107 | |
| A | ASP180 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| B | ARG54 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| B | TYR107 | |
| B | ASP180 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| A | ARG54 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| A | TYR107 | |
| A | LYS206 | |
| A | ASP180 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| B | TYR107 | |
| B | LYS206 | |
| B | ASP180 |
