eF-site ID 1a05-B PDB Code 1a05 Chain 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 null (LEU3_THIFE) Sequence B:  MKKIAIFAGDGIGPEIVAAARQVLDAVDQAAHLGLRCTEG LVGGAALDASDDPLPAASLQLAMAADAVILGAVGGPRWDA YPPAKRPEQGLLRLRKGLDLYANLRPAQIFPQLLDASPLR PELVRDVDILVVRELTGDIYFGQPRGLEVIDGKRRGFNTM VYDEDEIRRIAHVAFRAAQGRRKQLCSVDKANVLETTRLW REVVTEVARDYPDVRLSHMYVDNAAMQLIRAPAQFDVLLT GNMFGDILSDEASQLTGSIGMLPSASLGEGRAMYEPIHGS APDIAGQDKANPLATILSVAMMLRHSLNAEPWAQRVEAAV QRVLDQGLRTADIAAPGTPVIGTKAMGAAVVNALNLK Description Functional site 1) chain B residue 222 type sequence D description BINDING SITE FOR RESIDUE MG A 501 source : AC1 2) chain B residue 246 type sequence D description BINDING SITE FOR RESIDUE MG A 502 source : AC2 3) chain B residue 190 type sequence K description BINDING SITE FOR RESIDUE IPM A 401 source : AC3 4) chain B residue 193 type sequence V description BINDING SITE FOR RESIDUE IPM A 401 source : AC3 5) chain B residue 222 type sequence D description BINDING SITE FOR RESIDUE IPM A 401 source : AC3 6) chain B residue 95 type sequence R description BINDING SITE FOR RESIDUE IPM B 402 source : AC4 7) chain B residue 105 type sequence R description BINDING SITE FOR RESIDUE IPM B 402 source : AC4 8) chain B residue 133 type sequence R description BINDING SITE FOR RESIDUE IPM B 402 source : AC4 9) chain B residue 140 type sequence Y description BINDING SITE FOR RESIDUE IPM B 402 source : AC4 10) chain B residue 246 type sequence D description BINDING SITE FOR RESIDUE IPM B 402 source : AC4 11) chain B residue 140 type catalytic sequence Y description 371 source MCSA : MCSA2 12) chain B residue 190 type catalytic sequence K description 371 source MCSA : MCSA2 13) chain B residue 222 type catalytic sequence D description 371 source MCSA : MCSA2 14) chain B residue 246 type catalytic sequence D description 371 source MCSA : MCSA2 15) chain B residue 250 type catalytic sequence D description 371 source MCSA : MCSA2 16) chain B residue 250 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01033 source Swiss-Prot : SWS_FT_FI1 17) chain B residue 279 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01033 source Swiss-Prot : SWS_FT_FI1 18) chain B residue 75 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01033 source Swiss-Prot : SWS_FT_FI1 19) 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 20) 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 21) 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 22) 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 23) 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 24) 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 25) chain B residue 246 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9739088, ECO:0007744|PDB:1A05 source Swiss-Prot : SWS_FT_FI3

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