1X0L
Crystal structure of tetrameric homoisocitrate dehydrogenase from an extreme thermophile, Thermus thermophilus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004449 | molecular_function | isocitrate dehydrogenase (NAD+) activity |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0006102 | biological_process | isocitrate metabolic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009085 | biological_process | lysine biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
| A | 0033708 | molecular_function | isocitrate-homoisocitrate dehydrogenase activity |
| A | 0046394 | biological_process | carboxylic acid biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047046 | molecular_function | homoisocitrate dehydrogenase activity |
| B | 0004449 | molecular_function | isocitrate dehydrogenase (NAD+) activity |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0006102 | biological_process | isocitrate metabolic process |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009085 | biological_process | lysine biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
| B | 0033708 | molecular_function | isocitrate-homoisocitrate dehydrogenase activity |
| B | 0046394 | biological_process | carboxylic acid biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047046 | molecular_function | homoisocitrate dehydrogenase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27601325","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4YB4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 11 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"27601325","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4YB4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27601325","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4YB4","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for substrate specificity and discrimination against 3-isopropylmalate"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| A | TYR125 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| B | ASP204 | |
| B | LYS171 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| B | TYR125 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| A | ASP204 | |
| A | LYS171 |
