4WUO
Structure of the E270A Mutant Isopropylmalate dehydrogenase from Thermus thermophilus in complex with IPM, Mn and NADH
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue IPM A 401 |
| Chain | Residue |
| A | ARG94 |
| A | HOH542 |
| A | HOH543 |
| B | LYS185 |
| B | VAL188 |
| B | ASP217 |
| A | ARG104 |
| A | ARG132 |
| A | TYR139 |
| A | ASP241 |
| A | NAD402 |
| A | MN403 |
| A | HOH527 |
| A | HOH528 |
| site_id | AC2 |
| Number of Residues | 33 |
| Details | binding site for residue NAD A 402 |
| Chain | Residue |
| A | ILE11 |
| A | SER71 |
| A | VAL72 |
| A | GLY73 |
| A | GLY74 |
| A | GLU87 |
| A | LEU90 |
| A | LEU254 |
| A | GLY255 |
| A | VAL272 |
| A | HIS273 |
| A | GLY274 |
| A | SER275 |
| A | ALA276 |
| A | ASP278 |
| A | ILE279 |
| A | ASN286 |
| A | IPM401 |
| A | GOL408 |
| A | HOH529 |
| A | HOH537 |
| A | HOH538 |
| A | HOH542 |
| A | HOH549 |
| A | HOH553 |
| A | HOH571 |
| A | HOH592 |
| B | ASN187 |
| B | TYR215 |
| B | ALA218 |
| B | HIS222 |
| B | EOH402 |
| B | HOH505 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MN A 403 |
| Chain | Residue |
| A | ASP241 |
| A | IPM401 |
| A | HOH527 |
| A | HOH528 |
| B | ASP217 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue K A 404 |
| Chain | Residue |
| A | GLU65 |
| A | GOL410 |
| A | GOL414 |
| A | HOH517 |
| B | HOH501 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue MN A 405 |
| Chain | Residue |
| A | ASP217 |
| A | IPM415 |
| B | ASP241 |
| B | HOH506 |
| B | HOH507 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue EOH A 406 |
| Chain | Residue |
| A | LYS107 |
| A | VAL108 |
| A | PHE109 |
| A | LEU112 |
| A | PRO251 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue EOH A 407 |
| Chain | Residue |
| A | GLU155 |
| A | VAL183 |
| A | GLY236 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 408 |
| Chain | Residue |
| A | GLY73 |
| A | GLY74 |
| A | ASP78 |
| A | ARG85 |
| A | GLU87 |
| A | NAD402 |
| B | TYR215 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue GOL A 409 |
| Chain | Residue |
| A | GLY263 |
| A | GOL410 |
| site_id | AD1 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 410 |
| Chain | Residue |
| A | GLY263 |
| A | ARG264 |
| A | GLY265 |
| A | K404 |
| A | GOL409 |
| A | GOL414 |
| B | ALA29 |
| B | GLU30 |
| B | HOH501 |
| site_id | AD2 |
| Number of Residues | 1 |
| Details | binding site for residue EOH A 411 |
| Chain | Residue |
| A | GLU312 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue EOH A 412 |
| Chain | Residue |
| A | ARG174 |
| A | GLY205 |
| A | ILE284 |
| A | SER330 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue EOH A 413 |
| Chain | Residue |
| A | PRO105 |
| A | LYS107 |
| A | LEU256 |
| A | HOH600 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 414 |
| Chain | Residue |
| A | ALA301 |
| A | K404 |
| A | GOL410 |
| A | HOH505 |
| A | GLU65 |
| A | HIS300 |
| site_id | AD6 |
| Number of Residues | 14 |
| Details | binding site for residue IPM A 415 |
| Chain | Residue |
| A | LYS185 |
| A | VAL188 |
| A | ASP217 |
| A | MN405 |
| A | HOH561 |
| A | HOH609 |
| B | ARG94 |
| B | ARG104 |
| B | ARG132 |
| B | TYR139 |
| B | ASP241 |
| B | NAD401 |
| B | HOH506 |
| B | HOH507 |
| site_id | AD7 |
| Number of Residues | 32 |
| Details | binding site for residue NAD B 401 |
| Chain | Residue |
| A | ASN187 |
| A | TYR215 |
| A | ALA218 |
| A | MET221 |
| A | HIS222 |
| A | IPM415 |
| A | HOH559 |
| A | HOH565 |
| A | HOH570 |
| A | HOH609 |
| B | ILE11 |
| B | SER71 |
| B | VAL72 |
| B | GLY73 |
| B | GLY74 |
| B | GLU87 |
| B | LEU90 |
| B | LEU254 |
| B | GLY255 |
| B | HIS273 |
| B | GLY274 |
| B | SER275 |
| B | ALA276 |
| B | PRO277 |
| B | ASP278 |
| B | ILE279 |
| B | ASN286 |
| B | HOH508 |
| B | HOH515 |
| B | HOH516 |
| B | HOH519 |
| B | HOH555 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue EOH B 402 |
| Chain | Residue |
| A | SER253 |
| A | LEU254 |
| A | NAD402 |
| B | MET221 |
| B | ARG225 |
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 | 50 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7881901","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for catalysis"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for catalysis","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
