3R8W
Structure of 3-isopropylmalate dehydrogenase isoform 2 from Arabidopsis thaliana at 2.2 angstrom resolution
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 | 3 |
Details | BINDING SITE FOR RESIDUE ACT A 368 |
Chain | Residue |
A | LYS151 |
A | PHE161 |
B | GLU146 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACT A 369 |
Chain | Residue |
A | HIS169 |
A | ARG173 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT A 370 |
Chain | Residue |
A | GLU91 |
A | ARG98 |
A | ARG108 |
A | ARG136 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACT A 371 |
Chain | Residue |
A | ASP235 |
A | GLN238 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT A 372 |
Chain | Residue |
A | ILE15 |
A | ASN296 |
A | ASP337 |
A | HOH487 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACT B 368 |
Chain | Residue |
B | HIS169 |
B | ARG173 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACT B 369 |
Chain | Residue |
B | ASP235 |
B | GLN238 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACT B 370 |
Chain | Residue |
B | ASP254 |
B | ILE282 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACT B 371 |
Chain | Residue |
B | ASN296 |
B | ASP337 |
site_id | BC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE ACT B 372 |
Chain | Residue |
B | ARG207 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT B 373 |
Chain | Residue |
B | GLU91 |
B | ARG98 |
B | ARG108 |
B | ARG136 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT C 368 |
Chain | Residue |
C | ARG98 |
C | ARG108 |
C | ARG136 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT D 368 |
Chain | Residue |
D | GLU91 |
D | ARG98 |
D | ARG108 |
D | ARG136 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT D 369 |
Chain | Residue |
D | ASP235 |
D | LYS237 |
D | GLN238 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACT D 370 |
Chain | Residue |
D | ARG108 |
D | ASP254 |
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 | ASN246-MET265 |
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 | ILE76 | |
C | ASN196 | |
C | ASN227 | |
C | GLU280 | |
D | ILE76 | |
D | ASN196 | |
D | ASN227 | |
D | GLU280 | |
A | ASN196 | |
A | ASN227 | |
A | GLU280 | |
B | ILE76 | |
B | ASN196 | |
B | ASN227 | |
B | GLU280 | |
C | ILE76 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27137927, ECO:0007744|PDB:5J32 |
Chain | Residue | Details |
A | ARG98 | |
C | ARG108 | |
C | ARG136 | |
C | ASP226 | |
D | ARG98 | |
D | ARG108 | |
D | ARG136 | |
D | ASP226 | |
A | ARG108 | |
A | ARG136 | |
A | ASP226 | |
B | ARG98 | |
B | ARG108 | |
B | ARG136 | |
B | ASP226 | |
C | ARG98 |
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 | ASP250 | |
A | ASP254 | |
B | ASP250 | |
B | ASP254 | |
C | ASP250 | |
C | ASP254 | |
D | ASP250 | |
D | ASP254 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Confers substrate specificity => ECO:0000269|PubMed:21697089 |
Chain | Residue | Details |
A | LEU95 | |
B | LEU95 | |
C | LEU95 | |
D | LEU95 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | SITE: Important for catalysis => ECO:0000269|PubMed:27137927 |
Chain | Residue | Details |
A | TYR143 | |
A | LYS194 | |
B | TYR143 | |
B | LYS194 | |
C | TYR143 | |
C | LYS194 | |
D | TYR143 | |
D | LYS194 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | SITE: Essential for redox regulation => ECO:0000250|UniProtKB:Q9FMT1 |
Chain | Residue | Details |
A | CYS190 | |
A | CYS348 | |
B | CYS190 | |
B | CYS348 | |
C | CYS190 | |
C | CYS348 | |
D | CYS190 | |
D | CYS348 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9FMT1 |
Chain | Residue | Details |
A | SER32 | |
B | SER32 | |
C | SER32 | |
D | SER32 |