Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005777 | cellular_component | peroxisome |
A | 0005782 | cellular_component | peroxisomal matrix |
A | 0005829 | cellular_component | cytosol |
A | 0006097 | biological_process | glyoxylate cycle |
A | 0006099 | biological_process | tricarboxylic acid cycle |
A | 0006102 | biological_process | isocitrate metabolic process |
A | 0006103 | biological_process | 2-oxoglutarate metabolic process |
A | 0006739 | biological_process | NADP+ metabolic process |
A | 0006740 | biological_process | NADPH regeneration |
A | 0006749 | biological_process | glutathione metabolic process |
A | 0006979 | biological_process | response to oxidative stress |
A | 0008585 | biological_process | female gonad development |
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 | 0042803 | molecular_function | protein homodimerization activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0048545 | biological_process | response to steroid hormone |
A | 0050661 | molecular_function | NADP binding |
A | 0051287 | molecular_function | NAD binding |
A | 0060696 | biological_process | regulation of phospholipid catabolic process |
A | 0071071 | biological_process | regulation of phospholipid biosynthetic process |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005777 | cellular_component | peroxisome |
B | 0005782 | cellular_component | peroxisomal matrix |
B | 0005829 | cellular_component | cytosol |
B | 0006097 | biological_process | glyoxylate cycle |
B | 0006099 | biological_process | tricarboxylic acid cycle |
B | 0006102 | biological_process | isocitrate metabolic process |
B | 0006103 | biological_process | 2-oxoglutarate metabolic process |
B | 0006739 | biological_process | NADP+ metabolic process |
B | 0006740 | biological_process | NADPH regeneration |
B | 0006749 | biological_process | glutathione metabolic process |
B | 0006979 | biological_process | response to oxidative stress |
B | 0008585 | biological_process | female gonad development |
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 | 0042803 | molecular_function | protein homodimerization activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0048545 | biological_process | response to steroid hormone |
B | 0050661 | molecular_function | NADP binding |
B | 0051287 | molecular_function | NAD binding |
B | 0060696 | biological_process | regulation of phospholipid catabolic process |
B | 0071071 | biological_process | regulation of phospholipid biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 35 |
Details | binding site for residue NAP A 501 |
Chain | Residue |
A | LYS72 |
A | THR311 |
A | VAL312 |
A | THR313 |
A | ARG314 |
A | HIS315 |
A | ASN328 |
A | HOH601 |
A | HOH619 |
A | HOH625 |
A | HOH633 |
A | ALA74 |
A | HOH647 |
A | HOH672 |
A | HOH724 |
A | HOH728 |
A | HOH748 |
A | HOH749 |
A | HOH775 |
A | HOH780 |
A | HOH824 |
B | LEU250 |
A | THR75 |
B | ASP253 |
B | GLN257 |
B | LYS260 |
B | HOH625 |
B | HOH669 |
B | HOH700 |
A | ILE76 |
A | THR77 |
A | ARG82 |
A | ASN96 |
A | HIS309 |
A | GLY310 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue GOL A 502 |
Chain | Residue |
A | PRO206 |
A | GLU262 |
A | GLY263 |
A | GLY264 |
A | HOH777 |
site_id | AC3 |
Number of Residues | 33 |
Details | binding site for residue NAP B 501 |
Chain | Residue |
A | ASP253 |
A | GLN257 |
A | LYS260 |
A | HOH642 |
A | HOH689 |
B | LYS72 |
B | ALA74 |
B | THR75 |
B | THR77 |
B | ARG82 |
B | ASN96 |
B | ALA307 |
B | HIS309 |
B | GLY310 |
B | THR311 |
B | VAL312 |
B | THR313 |
B | ARG314 |
B | HIS315 |
B | ASN328 |
B | HOH606 |
B | HOH621 |
B | HOH624 |
B | HOH632 |
B | HOH644 |
B | HOH646 |
B | HOH692 |
B | HOH702 |
B | HOH715 |
B | HOH730 |
B | HOH734 |
B | HOH735 |
B | HOH767 |
Functional Information from PROSITE/UniProt
site_id | PS00470 |
Number of Residues | 20 |
Details | IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NYDGDVqSDsvAqgy.GSLGM |
Chain | Residue | Details |
A | ASN271-MET290 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 20 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"29923039","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5YZH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5YZI","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 18 |
Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"29923039","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5YZI","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"29923039","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5YZI","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"29923039","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"29923039","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | Site: {"description":"Critical for catalysis","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"O75874","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 8 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"23576753","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O75874","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |