eF-site ID 9icd-A PDB Code 9icd Chain A click to enlarge Title CATALYTIC MECHANISM OF NADP+-DEPENDENT ISOCITRATE DEHYDROGENASE: IMPLICATIONS FROM THE STRUCTURES OF MAGNESIUM-ISOCITRATE AND NADP+ COMPLEXES Classification OXIDOREDUCTASE (NAD(A)-CHOH(D)) Compound ISOCITRATE DEHYDROGENASE Source Escherichia coli (strain K12) (IDH_ECOLI) Sequence A:  SKVVVPAQGKKITLQNGKLNVPENPIIPYIEGDGIGVDVT PAMLKVVDAAVEKAYKGERKISWMEIYTGEKSTQVYGQDV WLPAETLDLIREYRVAIKGPLTTPVGGGIRSLNVALRQEL DLYICLRPVRYYQGTPSPVKHPELTDMVIFRENSEDIYAG IEWKADSADAEKVIKFLREEMGVKKIRFPEHCGIGIKPCS EEGTKRLVRAAIEYAIANDRDSVTLVHKGNIMKFTEGAFK DWGYQLAREEFGGELIDGGPWLKVKNPNTGKEIVIKDVIA DAFLQQILLRPAEYDVIACMNLNGDYISDALAAQVGGIGI APGANIGDECALFEATHGTAPKYAGQDKVNPGSIILSAEM MLRHMGWTEAADLIVKGMEGAINAKTVTYDFERLMDGAKL LKCSEFGDAIIENM Description Functional site 1) chain A residue 37 type sequence I description BINDING SITE FOR RESIDUE NAP A 417 source : AC1 2) chain A residue 292 type sequence R description BINDING SITE FOR RESIDUE NAP A 417 source : AC1 3) chain A residue 339 type sequence H description BINDING SITE FOR RESIDUE NAP A 417 source : AC1 4) chain A residue 340 type sequence G description BINDING SITE FOR RESIDUE NAP A 417 source : AC1 5) chain A residue 341 type sequence T description BINDING SITE FOR RESIDUE NAP A 417 source : AC1 6) chain A residue 342 type sequence A description BINDING SITE FOR RESIDUE NAP A 417 source : AC1 7) chain A residue 345 type sequence Y description BINDING SITE FOR RESIDUE NAP A 417 source : AC1 8) chain A residue 352 type sequence N description BINDING SITE FOR RESIDUE NAP A 417 source : AC1 9) chain A residue 391 type sequence Y description BINDING SITE FOR RESIDUE NAP A 417 source : AC1 10) chain A residue 395 type sequence R description BINDING SITE FOR RESIDUE NAP A 417 source : AC1 11) chain A residue 115 type BINDING sequence N description 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 source Swiss-Prot : SWS_FT_FI2 12) chain A residue 129 type BINDING sequence R description 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 source Swiss-Prot : SWS_FT_FI2 13) chain A residue 153 type BINDING sequence R description 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 source Swiss-Prot : SWS_FT_FI2 14) chain A residue 113 type BINDING sequence S description 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 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 391 type BINDING sequence Y description 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 source Swiss-Prot : SWS_FT_FI6 16) chain A residue 352 type BINDING sequence N description 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 source Swiss-Prot : SWS_FT_FI6 17) chain A residue 395 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:2682654, ECO:0000269|PubMed:7761851, ECO:0007744|PDB:1AI2, ECO:0007744|PDB:9ICD source Swiss-Prot : SWS_FT_FI7 18) chain A residue 242 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI9 19) chain A residue 100 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI9 20) chain A residue 113 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:2204109, ECO:0000269|PubMed:3112144 source Swiss-Prot : SWS_FT_FI10 21) chain A residue 142 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:18723842 source Swiss-Prot : SWS_FT_FI11 22) chain A residue 303-322 type prosite sequence NLNGDYISDALAAQVGGIGI description IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NLNGDYiSDalAaqv.GGIGI source prosite : PS00470 23) chain A residue 160 type catalytic sequence Y description 7 source MCSA : MCSA1 24) chain A residue 230 type catalytic sequence K description 7 source MCSA : MCSA1 25) chain A residue 283 type catalytic sequence D description 7 source MCSA : MCSA1 26) chain A residue 307 type catalytic sequence D description 7 source MCSA : MCSA1 27) chain A residue 104 type BINDING sequence T description 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 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 119 type BINDING sequence R description 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 source Swiss-Prot : SWS_FT_FI3 29) chain A residue 307 type BINDING sequence D description 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 source Swiss-Prot : SWS_FT_FI4 30) chain A residue 339 type BINDING sequence H description 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 source Swiss-Prot : SWS_FT_FI5 31) chain A residue 230 type SITE sequence K description Critical for catalysis => ECO:0000269|PubMed:7761851, ECO:0000269|PubMed:7819221 source Swiss-Prot : SWS_FT_FI8 32) chain A residue 160 type SITE sequence Y description Critical for catalysis => ECO:0000269|PubMed:7761851, ECO:0000269|PubMed:7819221 source Swiss-Prot : SWS_FT_FI8

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