eF-site ID 1a05-AB PDB Code 1a05 Chain A, B click to enlarge Title CRYSTAL STRUCTURE OF THE COMPLEX OF 3-ISOPROPYLMALATE DEHYDROGENASE FROM THIOBACILLUS FERROOXIDANS WITH 3-ISOPROPYLMALATE Classification OXIDOREDUCTASE Compound 3-ISOPROPYLMALATE DEHYDROGENASE Source Thiobacillus ferrooxidans (Acidithiobacillus ferrooxidans) (LEU3_THIFE) Sequence A:  MKKIAIFAGDGIGPEIVAAARQVLDAVDQAAHLGLRCTEG LVGGAALDASDDPLPAASLQLAMAADAVILGAVGGPRWDA YPPAKRPEQGLLRLRKGLDLYANLRPAQIFPQLLDASPLR PELVRDVDILVVRELTGDIYFGQPRGLEVIDGKRRGFNTM VYDEDEIRRIAHVAFRAAQGRRKQLCSVDKANVLETTRLW REVVTEVARDYPDVRLSHMYVDNAAMQLIRAPAQFDVLLT GNMFGDILSDEASQLTGSIGMLPSASLGEGRAMYEPIHGS APDIAGQDKANPLATILSVAMMLRHSLNAEPWAQRVEAAV QRVLDQGLRTADIAAPGTPVIGTKAMGAAVVNALNLK B:  MKKIAIFAGDGIGPEIVAAARQVLDAVDQAAHLGLRCTEG LVGGAALDASDDPLPAASLQLAMAADAVILGAVGGPRWDA YPPAKRPEQGLLRLRKGLDLYANLRPAQIFPQLLDASPLR PELVRDVDILVVRELTGDIYFGQPRGLEVIDGKRRGFNTM VYDEDEIRRIAHVAFRAAQGRRKQLCSVDKANVLETTRLW REVVTEVARDYPDVRLSHMYVDNAAMQLIRAPAQFDVLLT GNMFGDILSDEASQLTGSIGMLPSASLGEGRAMYEPIHGS APDIAGQDKANPLATILSVAMMLRHSLNAEPWAQRVEAAV QRVLDQGLRTADIAAPGTPVIGTKAMGAAVVNALNLK Description Functional site 1) chain A residue 246 type sequence D description BINDING SITE FOR RESIDUE MG A 501 source : AC1 2) chain B residue 222 type sequence D description BINDING SITE FOR RESIDUE MG A 501 source : AC1 3) chain A residue 222 type sequence D description BINDING SITE FOR RESIDUE MG A 502 source : AC2 4) chain B residue 246 type sequence D description BINDING SITE FOR RESIDUE MG A 502 source : AC2 5) chain A residue 88 type sequence E description BINDING SITE FOR RESIDUE IPM A 401 source : AC3 6) chain A residue 95 type sequence R description BINDING SITE FOR RESIDUE IPM A 401 source : AC3 7) chain A residue 105 type sequence R description BINDING SITE FOR RESIDUE IPM A 401 source : AC3 8) chain A residue 133 type sequence R description BINDING SITE FOR RESIDUE IPM A 401 source : AC3 9) chain A residue 140 type sequence Y description BINDING SITE FOR RESIDUE IPM A 401 source : AC3 10) chain A residue 246 type sequence D description BINDING SITE FOR RESIDUE IPM A 401 source : AC3 11) chain B residue 190 type sequence K description BINDING SITE FOR RESIDUE IPM A 401 source : AC3 12) chain B residue 193 type sequence V description BINDING SITE FOR RESIDUE IPM A 401 source : AC3 13) chain B residue 222 type sequence D description BINDING SITE FOR RESIDUE IPM A 401 source : AC3 14) chain A residue 190 type sequence K description BINDING SITE FOR RESIDUE IPM B 402 source : AC4 15) chain A residue 193 type sequence V description BINDING SITE FOR RESIDUE IPM B 402 source : AC4 16) chain A residue 222 type sequence D description BINDING SITE FOR RESIDUE IPM B 402 source : AC4 17) chain B residue 95 type sequence R description BINDING SITE FOR RESIDUE IPM B 402 source : AC4 18) chain B residue 105 type sequence R description BINDING SITE FOR RESIDUE IPM B 402 source : AC4 19) chain B residue 133 type sequence R description BINDING SITE FOR RESIDUE IPM B 402 source : AC4 20) chain B residue 140 type sequence Y description BINDING SITE FOR RESIDUE IPM B 402 source : AC4 21) chain B residue 246 type sequence D description BINDING SITE FOR RESIDUE IPM B 402 source : AC4 22) chain A residue 140 type catalytic sequence Y description 371 source MCSA : MCSA1 23) chain A residue 190 type catalytic sequence K description 371 source MCSA : MCSA1 24) chain A residue 222 type catalytic sequence D description 371 source MCSA : MCSA1 25) chain A residue 246 type catalytic sequence D description 371 source MCSA : MCSA1 26) chain A residue 250 type catalytic sequence D description 371 source MCSA : MCSA1 27) chain B residue 140 type catalytic sequence Y description 371 source MCSA : MCSA2 28) chain B residue 190 type catalytic sequence K description 371 source MCSA : MCSA2 29) chain B residue 222 type catalytic sequence D description 371 source MCSA : MCSA2 30) chain B residue 246 type catalytic sequence D description 371 source MCSA : MCSA2 31) chain B residue 250 type catalytic sequence D description 371 source MCSA : MCSA2 32) chain A residue 242-261 type prosite sequence NMFGDILSDEASQLTGSIGM description IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NMFGDIlSDeaSqlt.GSIGM source prosite : PS00470 33) chain A residue 75 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01033 source Swiss-Prot : SWS_FT_FI1 34) chain A residue 250 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01033 source Swiss-Prot : SWS_FT_FI1 35) chain A residue 279 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01033 source Swiss-Prot : SWS_FT_FI1 36) chain B residue 75 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01033 source Swiss-Prot : SWS_FT_FI1 37) chain B residue 250 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01033 source Swiss-Prot : SWS_FT_FI1 38) chain B residue 279 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01033 source Swiss-Prot : SWS_FT_FI1 39) chain A residue 95 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_01033, ECO:0000269|PubMed:9739088 source Swiss-Prot : SWS_FT_FI2 40) chain A residue 105 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_01033, ECO:0000269|PubMed:9739088 source Swiss-Prot : SWS_FT_FI2 41) chain A residue 133 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_01033, ECO:0000269|PubMed:9739088 source Swiss-Prot : SWS_FT_FI2 42) chain A residue 222 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01033, ECO:0000269|PubMed:9739088 source Swiss-Prot : SWS_FT_FI2 43) chain B residue 95 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_01033, ECO:0000269|PubMed:9739088 source Swiss-Prot : SWS_FT_FI2 44) chain B residue 105 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_01033, ECO:0000269|PubMed:9739088 source Swiss-Prot : SWS_FT_FI2 45) chain B residue 133 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_01033, ECO:0000269|PubMed:9739088 source Swiss-Prot : SWS_FT_FI2 46) chain B residue 222 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01033, ECO:0000269|PubMed:9739088 source Swiss-Prot : SWS_FT_FI2 47) chain A residue 246 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9739088, ECO:0007744|PDB:1A05 source Swiss-Prot : SWS_FT_FI3 48) chain B residue 246 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9739088, ECO:0007744|PDB:1A05 source Swiss-Prot : SWS_FT_FI3 49) chain A residue 140 type SITE sequence Y description Important for catalysis => ECO:0000255|HAMAP-Rule:MF_01033, ECO:0000305|PubMed:9739088 source Swiss-Prot : SWS_FT_FI4 50) chain A residue 190 type SITE sequence K description Important for catalysis => ECO:0000255|HAMAP-Rule:MF_01033, ECO:0000305|PubMed:9739088 source Swiss-Prot : SWS_FT_FI4 51) chain B residue 140 type SITE sequence Y description Important for catalysis => ECO:0000255|HAMAP-Rule:MF_01033, ECO:0000305|PubMed:9739088 source Swiss-Prot : SWS_FT_FI4 52) chain B residue 190 type SITE sequence K description Important for catalysis => ECO:0000255|HAMAP-Rule:MF_01033, ECO:0000305|PubMed:9739088 source Swiss-Prot : SWS_FT_FI4

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