4AJB
3D structure of E. coli Isocitrate Dehydrogenase K100M mutant in complex with Isocitrate, magnesium(II) and thioNADP
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 | 30 |
Details | BINDING SITE FOR RESIDUE TAP A 501 |
Chain | Residue |
A | LYS58 |
A | TYR345 |
A | VAL351 |
A | ASN352 |
A | TYR391 |
A | ASP392 |
A | ARG395 |
A | ICT502 |
A | HOH2167 |
A | HOH2169 |
A | HOH2172 |
A | LEU103 |
A | HOH2182 |
A | HOH2401 |
A | HOH2411 |
A | HOH2412 |
A | HOH2483 |
A | HOH2484 |
A | HOH2485 |
A | HOH2486 |
A | HOH2487 |
A | HOH2488 |
A | THR105 |
A | HOH2489 |
A | ARG292 |
A | THR338 |
A | HIS339 |
A | GLY340 |
A | THR341 |
A | ALA342 |
site_id | AC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE ICT A 502 |
Chain | Residue |
A | SER113 |
A | ARG119 |
A | ARG129 |
A | ARG153 |
A | TYR160 |
A | LYS230 |
A | ASN232 |
A | ASP283 |
A | ASP307 |
A | TAP501 |
A | MG503 |
A | HOH2172 |
A | HOH2182 |
A | HOH2200 |
A | HOH2393 |
A | HOH2484 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 503 |
Chain | Residue |
A | ASP283 |
A | ASP307 |
A | ICT502 |
A | HOH2199 |
A | HOH2393 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 504 |
Chain | Residue |
A | GLY108 |
A | GLY109 |
A | GLY110 |
A | LYS235 |
A | HOH2174 |
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 | SER113 | |
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 | MET100 | |
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 | SER113 |
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 | 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 |