eF-site ID 1ecq-B PDB Code 1ecq Chain B click to enlarge Title E. COLI GLUCARATE DEHYDRATASE BOUND TO 4-DEOXYGLUCARATE Classification LYASE Compound GLUCARATE DEHYDRATASE Source (GUDH_ECOLI) Sequence B:  FTTPVVTEMQVIPVAGHDSMLMNLSGAHAPFFTRNIVIIK DNSGHTGVGEIPGGEKIRKTLEDAIPLVVGKTLGEYKNVL TLVRNTFADRDAGGRGLQTFDLRTTIHVVTGIEAAMLDLL GQHLGVNVASLLGDGQQRSEVEMLGYLFFVGNRKATPLPY QSQPDDSCDWYRLRHEEAMTPDAVVRLAEAAYEKYGFNDF KLKGGVLAGEEEAESIVALAQRFPQARITLDPNGAWSLNE AIKIGKYLKGSLAYAEDPCGAEQGFSGREVMAEFRRATGL PTATNMIATDWRQMGHTLSLQSVDIPLADPHFWTMQGSVR VAQMCHEFGLTWGSHSNNHFDISLAMFTHVAAAAPGKITA IDTHWIWQEGNQRLTKEPFEIKGGLVQVPEKPGLGVEIDM DQVMKAHELYQKHGLGARDDAMGMQYLIPGWTFDNKRPCM VR Description Functional site 1) chain B residue 27 type sequence N description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 2) chain B residue 32 type sequence H description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 3) chain B residue 103 type sequence T description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 4) chain B residue 150 type sequence Y description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 5) chain B residue 152 type sequence F description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 6) chain B residue 205 type sequence K description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 7) chain B residue 207 type sequence K description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 8) chain B residue 235 type sequence D description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 9) chain B residue 237 type sequence N description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 10) chain B residue 260 type sequence E description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 11) chain B residue 289 type sequence N description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 12) chain B residue 339 type sequence H description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 13) chain B residue 340 type sequence S description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 14) chain B residue 341 type sequence N description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 15) chain B residue 368 type sequence H description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 16) chain B residue 422 type sequence R description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 17) chain B residue 235 type sequence D description BINDING SITE FOR RESIDUE MG B 498 source : AC6 18) chain B residue 260 type sequence E description BINDING SITE FOR RESIDUE MG B 498 source : AC6 19) chain B residue 289 type sequence N description BINDING SITE FOR RESIDUE MG B 498 source : AC6 20) chain B residue 302 type sequence L description BINDING SITE FOR RESIDUE IPA D 601 source : AC9 21) chain B residue 299 type sequence G description BINDING SITE FOR RESIDUE IPA B 603 source : BC2 22) chain B residue 303 type sequence S description BINDING SITE FOR RESIDUE IPA B 603 source : BC2 23) chain B residue 205 type catalytic sequence K description 451 source MCSA : MCSA2 24) chain B residue 207 type catalytic sequence K description 451 source MCSA : MCSA2 25) chain B residue 235 type catalytic sequence D description 451 source MCSA : MCSA2 26) chain B residue 237 type catalytic sequence N description 451 source MCSA : MCSA2 27) chain B residue 260 type catalytic sequence E description 451 source MCSA : MCSA2 28) chain B residue 289 type catalytic sequence N description 451 source MCSA : MCSA2 29) chain B residue 313 type catalytic sequence D description 451 source MCSA : MCSA2 30) chain B residue 339 type catalytic sequence H description 451 source MCSA : MCSA2 31) chain B residue 341 type catalytic sequence N description 451 source MCSA : MCSA2 32) chain B residue 207 type ACT_SITE sequence K description Proton acceptor => ECO:0000269|PubMed:11513584 source Swiss-Prot : SWS_FT_FI1 33) chain B residue 339 type ACT_SITE sequence H description Proton acceptor => ECO:0000269|PubMed:11513584 source Swiss-Prot : SWS_FT_FI1 34) chain B residue 103 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 35) chain B residue 150 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 36) chain B residue 205 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 37) chain B residue 289 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 38) chain B residue 339 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 39) chain B residue 368 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 40) chain B residue 422 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 41) chain B residue 32 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 42) chain B residue 235 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11513584 source Swiss-Prot : SWS_FT_FI3 43) chain B residue 266 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11513584 source Swiss-Prot : SWS_FT_FI3

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