2G4O
anomalous substructure of 3-ISOPROPYLMALATE DEHYDROGENASE
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 | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009098 | biological_process | L-leucine biosynthetic process |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0051287 | molecular_function | NAD binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003862 | molecular_function | 3-isopropylmalate dehydrogenase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0009098 | biological_process | L-leucine biosynthetic process |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0051287 | molecular_function | NAD binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003862 | molecular_function | 3-isopropylmalate dehydrogenase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0009098 | biological_process | L-leucine biosynthetic process |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0051287 | molecular_function | NAD binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0003862 | molecular_function | 3-isopropylmalate dehydrogenase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0009098 | biological_process | L-leucine biosynthetic process |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 D 801 |
| Chain | Residue |
| D | GLY104 |
| D | ASN112 |
| D | HOH868 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 802 |
| Chain | Residue |
| A | GLU47 |
| A | VAL48 |
| A | LEU49 |
| A | PRO50 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 803 |
| Chain | Residue |
| A | HOH859 |
| A | ARG165 |
| A | ARG168 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 804 |
| Chain | Residue |
| A | ALA67 |
| A | ILE68 |
| A | HOH830 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL B 805 |
| Chain | Residue |
| B | ARG165 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL C 806 |
| Chain | Residue |
| C | ARG165 |
| C | HOH835 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 807 |
| Chain | Residue |
| A | ARG121 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL D 808 |
| Chain | Residue |
| D | ARG165 |
| D | HOH916 |
Functional Information from PROSITE/UniProt
| site_id | PS00470 |
| Number of Residues | 20 |
| Details | IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NLFGDIiTDlaAavc.GGIGL |
| Chain | Residue | Details |
| A | ASN231-LEU250 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 72 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01035","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Site: {"description":"Important for catalysis","evidences":[{"source":"HAMAP-Rule","id":"MF_01035","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 | ASP211 | |
| A | LYS178 | |
| B | TYR128 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| A | TYR128 | |
| B | ASP211 | |
| B | LYS178 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| D | TYR128 | |
| C | ASP211 | |
| C | LYS178 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| C | TYR128 | |
| D | ASP211 | |
| D | LYS178 |
