4PG8
Crystal structure of S. aureus Homoserine Dehydrogenase at pH8.5
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004412 | molecular_function | homoserine dehydrogenase activity |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009086 | biological_process | methionine biosynthetic process |
| A | 0009088 | biological_process | threonine biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050661 | molecular_function | NADP binding |
| B | 0004412 | molecular_function | homoserine dehydrogenase activity |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009086 | biological_process | methionine biosynthetic process |
| B | 0009088 | biological_process | threonine biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue ACT A 501 |
| Chain | Residue |
| A | LEU242 |
| A | TYR244 |
| A | ASP269 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue ACT A 502 |
| Chain | Residue |
| A | VAL79 |
| A | MET80 |
| A | GLY81 |
| A | ALA103 |
| A | ASN104 |
| A | LYS105 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue ACT A 503 |
| Chain | Residue |
| A | GLU264 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue ACT A 504 |
| Chain | Residue |
| A | HIS382 |
| A | ARG383 |
| A | SER384 |
| A | HOH601 |
| A | HOH617 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 505 |
| Chain | Residue |
| A | GLY10 |
| A | LEU11 |
| A | ARG45 |
| A | ARG51 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue ACT A 506 |
| Chain | Residue |
| A | TYR281 |
| A | TYR297 |
| A | HOH714 |
| B | TYR285 |
| B | HOH647 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 507 |
| Chain | Residue |
| A | ASN5 |
| A | SER72 |
| A | ASP74 |
| B | GLU416 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 508 |
| Chain | Residue |
| A | GLN216 |
| A | VAL217 |
| A | GLY257 |
| A | VAL259 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue ACT A 509 |
| Chain | Residue |
| A | THR170 |
| A | ASN237 |
| A | ASP240 |
| A | HOH618 |
| B | PEG510 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue PEG A 510 |
| Chain | Residue |
| A | ASN221 |
| A | VAL223 |
| A | LYS224 |
| A | ARG225 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue ACT B 501 |
| Chain | Residue |
| B | VAL79 |
| B | MET80 |
| B | GLY81 |
| B | ALA103 |
| B | ASN104 |
| B | LYS105 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue ACT B 502 |
| Chain | Residue |
| A | HIS413 |
| B | ALA377 |
| B | LEU379 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue ACT B 503 |
| Chain | Residue |
| B | GLN216 |
| B | VAL217 |
| B | GLY257 |
| B | VAL259 |
| site_id | AD5 |
| Number of Residues | 2 |
| Details | binding site for residue ACT B 504 |
| Chain | Residue |
| B | LYS224 |
| B | GLU264 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue ACT B 505 |
| Chain | Residue |
| B | ASP240 |
| B | GLN241 |
| B | GLY243 |
| B | LYS270 |
| site_id | AD7 |
| Number of Residues | 2 |
| Details | binding site for residue ACT B 506 |
| Chain | Residue |
| B | HIS413 |
| B | GLY414 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue ACT B 507 |
| Chain | Residue |
| B | LYS113 |
| B | GLU116 |
| B | ASP117 |
| B | TYR211 |
| B | ASN215 |
| site_id | AD9 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 508 |
| Chain | Residue |
| B | HIS59 |
| B | THR61 |
| B | GLU66 |
| B | THR170 |
| B | LYS171 |
| B | GLN173 |
| B | HOH612 |
| B | HOH693 |
| site_id | AE1 |
| Number of Residues | 5 |
| Details | binding site for residue PEG B 509 |
| Chain | Residue |
| B | LEU11 |
| B | ARG45 |
| B | ASP46 |
| B | ARG51 |
| B | MET80 |
| site_id | AE2 |
| Number of Residues | 5 |
| Details | binding site for residue PEG B 510 |
| Chain | Residue |
| A | ASP240 |
| A | LYS270 |
| A | ACT509 |
| B | ASP46 |
| B | HOH625 |
| site_id | AE3 |
| Number of Residues | 4 |
| Details | binding site for residue DMS B 511 |
| Chain | Residue |
| B | LEU242 |
| B | ASP269 |
| B | ARG386 |
| B | HOH661 |
Functional Information from PROSITE/UniProt
| site_id | PS01042 |
| Number of Residues | 23 |
| Details | HOMOSER_DHGENASE Homoserine dehydrogenase signature. AkrlGFAea.DPtdDVeGvDaarK |
| Chain | Residue | Details |
| A | ALA183-LYS205 |
