1HJ6
ISOCITRATE DEHYDROGENASE S113E MUTANT COMPLEXED WITH ISOPROPYLMALATE, NADP+ AND MAGNESIUM (FLASH-COOLED)
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 | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006097 | biological_process | glyoxylate cycle |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0006979 | biological_process | response to oxidative stress |
| 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 | 0022900 | biological_process | electron transport chain |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051287 | molecular_function | NAD binding |
| A | 0097216 | molecular_function | guanosine tetraphosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A1421 |
| Chain | Residue |
| A | ASP283 |
| A | ASP307 |
| A | IPM1419 |
| A | HOH2187 |
| A | HOH2201 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE IPM A1419 |
| Chain | Residue |
| A | TYR160 |
| A | LYS230 |
| A | ILE233 |
| A | ASP283 |
| A | ASP307 |
| A | NAP1420 |
| A | MG1421 |
| A | HOH2226 |
| A | GLU113 |
| A | ARG119 |
| A | ARG129 |
| A | ARG153 |
| site_id | AC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAP A1420 |
| Chain | Residue |
| A | GLU60 |
| A | LYS100 |
| A | PRO102 |
| A | LEU103 |
| A | THR104 |
| A | ASN115 |
| A | GLN288 |
| A | ARG292 |
| A | ILE320 |
| A | GLY321 |
| A | GLU336 |
| A | THR338 |
| A | HIS339 |
| A | GLY340 |
| A | THR341 |
| A | ALA342 |
| A | TYR345 |
| A | VAL351 |
| A | ASN352 |
| A | TYR391 |
| A | ASP392 |
| A | IPM1419 |
| A | HOH2227 |
| A | HOH2228 |
| A | HOH2230 |
| A | HOH2232 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A1417 |
| Chain | Residue |
| A | ARG96 |
| A | ILE328 |
| A | GLY329 |
| A | ASP330 |
| A | CYS332 |
| A | ALA333 |
| A | HIS366 |
| A | GOL1418 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A1418 |
| Chain | Residue |
| A | PHE152 |
| A | HIS366 |
| A | GOL1417 |
| A | HOH2142 |
| A | HOH2206 |
Functional Information from PROSITE/UniProt
| site_id | PS00470 |
| Number of Residues | 20 |
| Details | IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NLNGDYiSDalAaqv.GGIGI |
| Chain | Residue | Details |
| A | ASN303-ILE322 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:2682654, ECO:0000269|PubMed:7761851, ECO:0007744|PDB:1AI2, ECO:0007744|PDB:1HJ6, ECO:0007744|PDB:1IDE, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJR |
| Chain | Residue | Details |
| A | THR104 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10623532, ECO:0000269|PubMed:2204109, ECO:0007744|PDB:1AI3, ECO:0007744|PDB:1CW1, ECO:0007744|PDB:1CW7, ECO:0007744|PDB:1GRP, ECO:0007744|PDB:1P8F, ECO:0007744|PDB:1PB1, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJA, ECO:0007744|PDB:4AJB, ECO:0007744|PDB:4AJS, ECO:0007744|PDB:4BNP, ECO:0007744|PDB:5ICD, ECO:0007744|PDB:8ICD |
| Chain | Residue | Details |
| A | GLU113 | |
| A | ASN115 | |
| A | ARG129 | |
| A | ARG153 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10623532, ECO:0000269|PubMed:2204109, ECO:0007744|PDB:1AI3, ECO:0007744|PDB:1CW7, ECO:0007744|PDB:1GRP, ECO:0007744|PDB:1P8F, ECO:0007744|PDB:1PB1, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJA, ECO:0007744|PDB:4AJB, ECO:0007744|PDB:4AJS, ECO:0007744|PDB:4BNP, ECO:0007744|PDB:5ICD, ECO:0007744|PDB:8ICD |
| Chain | Residue | Details |
| A | ARG119 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:2204109, ECO:0000269|PubMed:7761851, ECO:0007744|PDB:1AI3, ECO:0007744|PDB:1BL5, ECO:0007744|PDB:1GRP, ECO:0007744|PDB:1HJ6, ECO:0007744|PDB:1IDC, ECO:0007744|PDB:1P8F, ECO:0007744|PDB:4AJB, ECO:0007744|PDB:4AJR, ECO:0007744|PDB:4AJS, ECO:0007744|PDB:4BNP, ECO:0007744|PDB:8ICD |
| Chain | Residue | Details |
| A | ASP307 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:2682654, ECO:0000269|PubMed:7761851, ECO:0007744|PDB:1AI2, ECO:0007744|PDB:1BL5, ECO:0007744|PDB:1HJ6, ECO:0007744|PDB:1IDE, ECO:0007744|PDB:1ISO, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJR, ECO:0007744|PDB:9ICD |
| Chain | Residue | Details |
| A | HIS339 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:2682654, ECO:0000269|PubMed:7761851, ECO:0007744|PDB:1AI2, ECO:0007744|PDB:1BL5, ECO:0007744|PDB:1HJ6, ECO:0007744|PDB:1IDE, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJR, ECO:0007744|PDB:9ICD |
| Chain | Residue | Details |
| A | ASN352 | |
| A | TYR391 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:2682654, ECO:0000269|PubMed:7761851, ECO:0007744|PDB:1AI2, ECO:0007744|PDB:9ICD |
| Chain | Residue | Details |
| A | ARG395 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | SITE: Critical for catalysis => ECO:0000269|PubMed:7761851, ECO:0000269|PubMed:7819221 |
| Chain | Residue | Details |
| A | TYR160 | |
| A | LYS230 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122 |
| Chain | Residue | Details |
| A | LYS100 | |
| A | LYS242 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:2204109, ECO:0000269|PubMed:3112144 |
| Chain | Residue | Details |
| A | GLU113 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
| Chain | Residue | Details |
| A | LYS142 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| A | TYR160 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| A | ASP283 | |
| A | LYS230 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 7 |
| Chain | Residue | Details |
| A | TYR160 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | LYS230 | electrostatic stabiliser, proton acceptor, proton donor, proton relay |
| A | ASP283 | electrostatic stabiliser, proton acceptor, proton donor |
| A | ASP307 | metal ligand |
