2Y42
Structure of Isopropylmalate dehydrogenase from Thermus thermophilus - complex with NADH and Mn
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003862 | molecular_function | 3-isopropylmalate dehydrogenase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| A | 0009098 | biological_process | L-leucine biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051287 | molecular_function | NAD binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003862 | molecular_function | 3-isopropylmalate dehydrogenase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| B | 0009098 | biological_process | L-leucine biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051287 | molecular_function | NAD binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003862 | molecular_function | 3-isopropylmalate dehydrogenase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| C | 0009098 | biological_process | L-leucine biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051287 | molecular_function | NAD binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0003862 | molecular_function | 3-isopropylmalate dehydrogenase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0008652 | biological_process | amino acid biosynthetic process |
| D | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| D | 0009098 | biological_process | L-leucine biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BCN A 501 |
| Chain | Residue |
| A | ARG104 |
| A | ASP241 |
| A | ASP245 |
| A | MN999 |
| B | ASP217 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE NAD A 900 |
| Chain | Residue |
| A | HIS273 |
| A | GLY274 |
| A | SER275 |
| A | ALA276 |
| A | ASP278 |
| A | ASN286 |
| A | HOH2042 |
| A | GLU87 |
| A | LEU90 |
| A | LEU254 |
| A | VAL272 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN A 999 |
| Chain | Residue |
| A | ASP241 |
| A | ASP245 |
| A | BCN501 |
| B | ASP217 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BCN B 501 |
| Chain | Residue |
| A | ASP217 |
| A | MET221 |
| B | ARG104 |
| B | ASP241 |
| B | ASP245 |
| B | MN999 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE NAD B 900 |
| Chain | Residue |
| B | ILE11 |
| B | VAL72 |
| B | GLY73 |
| B | GLY74 |
| B | ASP78 |
| B | GLY255 |
| B | HIS273 |
| B | GLY274 |
| B | SER275 |
| B | ALA276 |
| B | ASP278 |
| B | ILE279 |
| B | ASN286 |
| B | HOH2044 |
| B | HOH2061 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN B 999 |
| Chain | Residue |
| A | ASP217 |
| B | ASP241 |
| B | ASP245 |
| B | BCN501 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BCN B 1502 |
| Chain | Residue |
| A | ARG225 |
| B | VAL249 |
| B | GLY252 |
| B | SER253 |
| B | LEU254 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BCN C 501 |
| Chain | Residue |
| C | ARG104 |
| C | ASP241 |
| C | ASP245 |
| C | MN999 |
| D | ASP217 |
| site_id | AC9 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE NAD C 900 |
| Chain | Residue |
| C | VAL72 |
| C | GLY73 |
| C | GLY74 |
| C | ASP78 |
| C | LEU90 |
| C | LEU254 |
| C | VAL272 |
| C | HIS273 |
| C | GLY274 |
| C | SER275 |
| C | ALA276 |
| C | ASP278 |
| C | ILE279 |
| C | ALA285 |
| C | ASN286 |
| C | HOH2024 |
| C | HOH2074 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN C 999 |
| Chain | Residue |
| C | ASP241 |
| C | ASP245 |
| C | BCN501 |
| D | ASP217 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BCN D 501 |
| Chain | Residue |
| C | ASP217 |
| D | ASP241 |
| D | ASP245 |
| D | MN999 |
| site_id | BC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE NAD D 900 |
| Chain | Residue |
| D | ILE11 |
| D | VAL72 |
| D | ASP78 |
| D | GLU87 |
| D | HIS273 |
| D | GLY274 |
| D | SER275 |
| D | ALA276 |
| D | ASP278 |
| D | ILE279 |
| D | ASN286 |
| D | HOH2058 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN D 999 |
| Chain | Residue |
| C | ASP217 |
| D | ASP241 |
| D | ASP245 |
| D | BCN501 |
Functional Information from PROSITE/UniProt
| site_id | PS00470 |
| Number of Residues | 20 |
| Details | IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NIFGDIlSDlaSvlp.GSLGL |
| Chain | Residue | Details |
| A | ASN237-LEU256 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 100 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7881901","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Site: {"description":"Important for catalysis"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Site: {"description":"Important for catalysis","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
