3AH3
Crystal structure of LR5-1, 3-isopropylmalate dehydrogenase created by directed evolution
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 | 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 | 0046394 | biological_process | carboxylic acid biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047046 | molecular_function | homoisocitrate dehydrogenase activity |
| C | 0004449 | molecular_function | isocitrate dehydrogenase (NAD+) activity |
| C | 0006099 | biological_process | tricarboxylic acid cycle |
| C | 0006102 | biological_process | isocitrate metabolic process |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0009085 | biological_process | lysine biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
| C | 0046394 | biological_process | carboxylic acid biosynthetic process |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0047046 | molecular_function | homoisocitrate dehydrogenase activity |
| D | 0004449 | molecular_function | isocitrate dehydrogenase (NAD+) activity |
| D | 0006099 | biological_process | tricarboxylic acid cycle |
| D | 0006102 | biological_process | isocitrate metabolic process |
| D | 0008652 | biological_process | amino acid biosynthetic process |
| D | 0009085 | biological_process | lysine biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
| D | 0046394 | biological_process | carboxylic acid biosynthetic process |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0047046 | molecular_function | homoisocitrate dehydrogenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 335 |
| Chain | Residue |
| A | ARG131 |
| C | LYS144 |
| C | LEU181 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 336 |
| Chain | Residue |
| A | GLU298 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 337 |
| Chain | Residue |
| A | ILE157 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 338 |
| Chain | Residue |
| A | ILE157 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 339 |
| Chain | Residue |
| A | ASN273 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 335 |
| Chain | Residue |
| D | LYS144 |
| D | LEU181 |
| B | ARG131 |
| B | HOH413 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO B 336 |
| Chain | Residue |
| B | GLU298 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO B 337 |
| Chain | Residue |
| B | ILE157 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 339 |
| Chain | Residue |
| B | ALA272 |
| B | ASN273 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 335 |
| Chain | Residue |
| A | LYS144 |
| A | LEU181 |
| C | ARG131 |
| C | HOH351 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO C 336 |
| Chain | Residue |
| C | ASP286 |
| C | GLU298 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 D 335 |
| Chain | Residue |
| B | LYS144 |
| D | ARG131 |
| D | HOH365 |
| site_id | BC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO D 336 |
| Chain | Residue |
| D | ASP286 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 36 |
| 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 | 24 |
| 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 | 12 |
| 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 | 4 |
| Details | Site: {"description":"Important for substrate specificity and discrimination against 3-isopropylmalate"} |
| Chain | Residue | Details |
