5J34
Isopropylmalate dehydrogenase K232M mutant
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 | 0005829 | cellular_component | cytosol |
A | 0009098 | biological_process | L-leucine biosynthetic process |
A | 0009507 | cellular_component | chloroplast |
A | 0009536 | cellular_component | plastid |
A | 0009553 | biological_process | embryo sac development |
A | 0009555 | biological_process | pollen development |
A | 0009570 | cellular_component | chloroplast stroma |
A | 0009941 | cellular_component | chloroplast envelope |
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 | 0042803 | molecular_function | protein homodimerization activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0051287 | molecular_function | NAD binding |
A | 0070403 | molecular_function | NAD+ binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0003862 | molecular_function | 3-isopropylmalate dehydrogenase activity |
B | 0005829 | cellular_component | cytosol |
B | 0009098 | biological_process | L-leucine biosynthetic process |
B | 0009507 | cellular_component | chloroplast |
B | 0009536 | cellular_component | plastid |
B | 0009553 | biological_process | embryo sac development |
B | 0009555 | biological_process | pollen development |
B | 0009570 | cellular_component | chloroplast stroma |
B | 0009941 | cellular_component | chloroplast envelope |
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 | 0042803 | molecular_function | protein homodimerization activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0051287 | molecular_function | NAD binding |
B | 0070403 | molecular_function | NAD+ binding |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0003862 | molecular_function | 3-isopropylmalate dehydrogenase activity |
C | 0005829 | cellular_component | cytosol |
C | 0009098 | biological_process | L-leucine biosynthetic process |
C | 0009507 | cellular_component | chloroplast |
C | 0009536 | cellular_component | plastid |
C | 0009553 | biological_process | embryo sac development |
C | 0009555 | biological_process | pollen development |
C | 0009570 | cellular_component | chloroplast stroma |
C | 0009941 | cellular_component | chloroplast envelope |
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 | 0042803 | molecular_function | protein homodimerization activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0051287 | molecular_function | NAD binding |
C | 0070403 | molecular_function | NAD+ binding |
D | 0000287 | molecular_function | magnesium ion binding |
D | 0003862 | molecular_function | 3-isopropylmalate dehydrogenase activity |
D | 0005829 | cellular_component | cytosol |
D | 0009098 | biological_process | L-leucine biosynthetic process |
D | 0009507 | cellular_component | chloroplast |
D | 0009536 | cellular_component | plastid |
D | 0009553 | biological_process | embryo sac development |
D | 0009555 | biological_process | pollen development |
D | 0009570 | cellular_component | chloroplast stroma |
D | 0009941 | cellular_component | chloroplast envelope |
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 | 0042803 | molecular_function | protein homodimerization activity |
D | 0046872 | molecular_function | metal ion binding |
D | 0051287 | molecular_function | NAD binding |
D | 0070403 | molecular_function | NAD+ binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue MG A 501 |
Chain | Residue |
A | ASP288 |
A | ASP292 |
A | HOH691 |
A | HOH714 |
A | HOH778 |
C | ASP264 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 502 |
Chain | Residue |
A | GLY302 |
A | HIS321 |
A | ASN334 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue SO4 A 503 |
Chain | Residue |
A | LYS130 |
A | GLN134 |
A | HOH612 |
A | HOH659 |
A | HOH757 |
B | LYS354 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue SO4 A 504 |
Chain | Residue |
A | ARG136 |
A | ARG146 |
A | ARG174 |
A | HOH610 |
A | HOH691 |
A | HOH714 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue MG B 501 |
Chain | Residue |
B | ASP288 |
B | ASP292 |
B | HOH662 |
B | HOH665 |
B | HOH753 |
D | ASP264 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue SO4 B 502 |
Chain | Residue |
B | ARG136 |
B | ARG146 |
B | ARG174 |
B | HOH611 |
B | HOH662 |
B | HOH665 |
B | HOH800 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue MG C 501 |
Chain | Residue |
A | ASP264 |
C | ASP288 |
C | ASP292 |
C | HOH644 |
C | HOH656 |
C | HOH789 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue SO4 C 502 |
Chain | Residue |
C | ARG136 |
C | ARG146 |
C | ARG174 |
C | HOH607 |
C | HOH644 |
C | HOH656 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue MG D 501 |
Chain | Residue |
B | ASP264 |
D | ASP288 |
D | ASP292 |
D | HOH663 |
D | HOH674 |
D | HOH745 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue SO4 D 502 |
Chain | Residue |
D | ARG136 |
D | ARG146 |
D | ARG174 |
D | HOH606 |
D | HOH663 |
D | HOH674 |
Functional Information from PROSITE/UniProt
site_id | PS00470 |
Number of Residues | 20 |
Details | IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NIFGDIlSDeaSmit.GSIGM |
Chain | Residue | Details |
A | ASN284-MET303 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27137927, ECO:0007744|PDB:5J33 |
Chain | Residue | Details |
A | ILE114 | |
C | ASN234 | |
C | ASN265 | |
C | GLU318 | |
D | ILE114 | |
D | ASN234 | |
D | ASN265 | |
D | GLU318 | |
A | ASN234 | |
A | ASN265 | |
A | GLU318 | |
B | ILE114 | |
B | ASN234 | |
B | ASN265 | |
B | GLU318 | |
C | ILE114 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27137927, ECO:0007744|PDB:5J32 |
Chain | Residue | Details |
A | ARG136 | |
C | ARG146 | |
C | ARG174 | |
C | ASP264 | |
D | ARG136 | |
D | ARG146 | |
D | ARG174 | |
D | ASP264 | |
A | ARG146 | |
A | ARG174 | |
A | ASP264 | |
B | ARG136 | |
B | ARG146 | |
B | ARG174 | |
B | ASP264 | |
C | ARG136 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27137927, ECO:0007744|PDB:5J32, ECO:0007744|PDB:5J33, ECO:0007744|PDB:5J34 |
Chain | Residue | Details |
A | ASP288 | |
A | ASP292 | |
B | ASP288 | |
B | ASP292 | |
C | ASP288 | |
C | ASP292 | |
D | ASP288 | |
D | ASP292 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Confers substrate specificity => ECO:0000269|PubMed:21697089 |
Chain | Residue | Details |
A | LEU133 | |
B | LEU133 | |
C | LEU133 | |
D | LEU133 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | SITE: Important for catalysis => ECO:0000269|PubMed:27137927 |
Chain | Residue | Details |
A | TYR181 | |
A | MET232 | |
B | TYR181 | |
B | MET232 | |
C | TYR181 | |
C | MET232 | |
D | TYR181 | |
D | MET232 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | SITE: Essential for redox regulation => ECO:0000250|UniProtKB:Q9FMT1 |
Chain | Residue | Details |
A | CYS228 | |
A | CYS386 | |
B | CYS228 | |
B | CYS386 | |
C | CYS228 | |
C | CYS386 | |
D | CYS228 | |
D | CYS386 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9FMT1 |
Chain | Residue | Details |
A | SER70 | |
B | SER70 | |
C | SER70 | |
D | SER70 |