1CNZ
3-ISOPROPYLMALATE DEHYDROGENASE (IPMDH) FROM SALMONELLA TYPHIMURIUM
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 | 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 | 0046872 | molecular_function | metal ion binding |
| B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 801 |
| Chain | Residue |
| A | ASP251 |
| A | ASP255 |
| A | SO4902 |
| A | HOH1054 |
| A | HOH1055 |
| B | ASP227 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN B 802 |
| Chain | Residue |
| B | HOH968 |
| A | ASP227 |
| B | ASP251 |
| B | ASP255 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 901 |
| Chain | Residue |
| A | ARG152 |
| B | LEU24 |
| B | ARG31 |
| B | THR40 |
| B | HIS42 |
| B | HOH1120 |
| B | HOH1124 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 902 |
| Chain | Residue |
| A | GLU91 |
| A | ARG99 |
| A | ARG138 |
| A | TYR145 |
| A | ASP251 |
| A | MN801 |
| A | HOH1053 |
| B | LYS195 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 903 |
| Chain | Residue |
| A | LYS103 |
| A | PHE170 |
| A | ARG174 |
| A | HOH929 |
| A | HOH931 |
| A | HOH1047 |
| B | ARG188 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 904 |
| Chain | Residue |
| B | ARG99 |
| B | ARG138 |
| B | HOH964 |
| B | HOH1219 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 905 |
| Chain | Residue |
| B | HIS55 |
| B | PRO58 |
| B | LYS59 |
| B | HOH924 |
| B | HOH954 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 906 |
| Chain | Residue |
| B | LYS103 |
| B | ARG174 |
| B | HOH1161 |
| B | HOH1176 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 907 |
| Chain | Residue |
| A | HIS168 |
| A | HOH1049 |
| B | LYS160 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 908 |
| Chain | Residue |
| A | ARG177 |
| A | GLU181 |
| A | ARG184 |
| A | THR215 |
| A | TYR216 |
| B | LYS214 |
| B | THR215 |
Functional Information from PROSITE/UniProt
| site_id | PS00470 |
| Number of Residues | 20 |
| Details | IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NLFGDIlSDecAmit.GSMGM |
| Chain | Residue | Details |
| A | ASN247-MET266 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 58 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01033","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9086278","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CNZ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Site: {"description":"Important for catalysis","evidences":[{"source":"HAMAP-Rule","id":"MF_01033","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| A | LYS195 | |
| A | ASP227 | |
| B | TYR145 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| A | TYR145 | |
| B | LYS195 | |
| B | ASP227 |
