1TVE
Homoserine Dehydrogenase in complex with 4-(4-hydroxy-3-isopropylphenylthio)-2-isopropylphenol
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004412 | molecular_function | homoserine dehydrogenase activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009067 | biological_process | aspartate family amino acid biosynthetic process |
| A | 0009086 | biological_process | methionine biosynthetic process |
| A | 0009088 | biological_process | threonine biosynthetic process |
| A | 0009090 | biological_process | homoserine biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0050661 | molecular_function | NADP binding |
| A | 0070403 | molecular_function | NAD+ binding |
| B | 0004412 | molecular_function | homoserine dehydrogenase activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009067 | biological_process | aspartate family amino acid biosynthetic process |
| B | 0009086 | biological_process | methionine biosynthetic process |
| B | 0009088 | biological_process | threonine biosynthetic process |
| B | 0009090 | biological_process | homoserine biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0050661 | molecular_function | NADP binding |
| B | 0070403 | molecular_function | NAD+ binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 178 A 1360 |
| Chain | Residue |
| A | GLY175 |
| A | THR176 |
| A | TYR206 |
| A | ASP214 |
| A | ASP219 |
| A | LYS223 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 178 B 2360 |
| Chain | Residue |
| B | TYR206 |
| B | ASP214 |
| B | ASP219 |
| B | LYS223 |
| B | SER174 |
| B | GLY175 |
| B | THR176 |
Functional Information from PROSITE/UniProt
| site_id | PS01042 |
| Number of Residues | 23 |
| Details | HOMOSER_DHGENASE Homoserine dehydrogenase signature. AkklGYTep.DPrdDLnGlDvarK |
| Chain | Residue | Details |
| A | ALA201-LYS223 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PIRSR","id":"PIRSR036497-1","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10700284","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EBF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EBU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"O58802","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10700284","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EBF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10700284","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14583265","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EBF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EBU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Q7G","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"F9VNG5","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10700284","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EBU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ebf |
| Chain | Residue | Details |
| A | LYS223 | |
| A | ASP219 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ebf |
| Chain | Residue | Details |
| B | LYS223 | |
| B | ASP219 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 521 |
| Chain | Residue | Details |
| A | ASP219 | electrostatic stabiliser |
| A | LYS223 | proton shuttle (general acid/base) |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 521 |
| Chain | Residue | Details |
| B | ASP219 | electrostatic stabiliser |
| B | LYS223 | proton shuttle (general acid/base) |
