eF-site ID 1ecq-C PDB Code 1ecq Chain C click to enlarge Title E. COLI GLUCARATE DEHYDRATASE BOUND TO 4-DEOXYGLUCARATE Classification LYASE Compound GLUCARATE DEHYDRATASE Source (GUDH_ECOLI) Sequence C:  QFTTPVVTEMQVIPVAGHDSMLMNLSGAHAPFFTRNIVII KDNSGHTGVGEIPGGEKIRKTLEDAIPLVVGKTLGEYKNV LTLVRNTFADRDAGGRGLQTFDLRTTIHVVTGIEAAMLDL LGQHLGVNVASLLGDGQQRSEVEMLGYLFFVGNRKATPLP YQSQPDDSCDWYRLRHEEAMTPDAVVRLAEAAYEKYGFND FKLKGGVLAGEEEAESIVALAQRFPQARITLDPNGAWSLN EAIKIGKYLKGSLAYAEDPCGAEQGFSGREVMAEFRRATG LPTATNMIATDWRQMGHTLSLQSVDIPLADPHFWTMQGSV RVAQMCHEFGLTWGSHSNNHFDISLAMFTHVAAAAPGKIT AIDTHWIWQEGNQRLTKEPFEIKGGLVQVPEKPGLGVEID MDQVMKAHELYQKHGLGARDDAMGMQYLIPGWTFDNKRPC MVR Description Functional site 1) chain C residue 27 type sequence N description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 2) chain C residue 32 type sequence H description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 3) chain C residue 103 type sequence T description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 4) chain C residue 104 type sequence F description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 5) chain C residue 150 type sequence Y description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 6) chain C residue 205 type sequence K description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 7) chain C residue 207 type sequence K description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 8) chain C residue 235 type sequence D description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 9) chain C residue 237 type sequence N description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 10) chain C residue 260 type sequence E description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 11) chain C residue 289 type sequence N description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 12) chain C residue 339 type sequence H description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 13) chain C residue 340 type sequence S description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 14) chain C residue 341 type sequence N description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 15) chain C residue 368 type sequence H description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 16) chain C residue 422 type sequence R description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 17) chain C residue 205 type sequence K description BINDING SITE FOR RESIDUE MG C 498 source : AC7 18) chain C residue 235 type sequence D description BINDING SITE FOR RESIDUE MG C 498 source : AC7 19) chain C residue 260 type sequence E description BINDING SITE FOR RESIDUE MG C 498 source : AC7 20) chain C residue 289 type sequence N description BINDING SITE FOR RESIDUE MG C 498 source : AC7 21) chain C residue 299 type sequence G description BINDING SITE FOR RESIDUE IPA A 602 source : BC1 22) chain C residue 303 type sequence S description BINDING SITE FOR RESIDUE IPA A 602 source : BC1 23) chain C residue 302 type sequence L description BINDING SITE FOR RESIDUE IPA C 604 source : BC3 24) chain C residue 332 type sequence F description BINDING SITE FOR RESIDUE IPA C 604 source : BC3 25) chain C residue 205 type catalytic sequence K description 451 source MCSA : MCSA3 26) chain C residue 207 type catalytic sequence K description 451 source MCSA : MCSA3 27) chain C residue 235 type catalytic sequence D description 451 source MCSA : MCSA3 28) chain C residue 237 type catalytic sequence N description 451 source MCSA : MCSA3 29) chain C residue 260 type catalytic sequence E description 451 source MCSA : MCSA3 30) chain C residue 289 type catalytic sequence N description 451 source MCSA : MCSA3 31) chain C residue 313 type catalytic sequence D description 451 source MCSA : MCSA3 32) chain C residue 339 type catalytic sequence H description 451 source MCSA : MCSA3 33) chain C residue 341 type catalytic sequence N description 451 source MCSA : MCSA3 34) chain C residue 207 type ACT_SITE sequence K description Proton acceptor => ECO:0000269|PubMed:11513584 source Swiss-Prot : SWS_FT_FI1 35) chain C residue 339 type ACT_SITE sequence H description Proton acceptor => ECO:0000269|PubMed:11513584 source Swiss-Prot : SWS_FT_FI1 36) chain C residue 32 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 37) chain C residue 103 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 38) chain C residue 150 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 39) chain C residue 205 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 40) chain C residue 289 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 41) chain C residue 339 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 42) chain C residue 368 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 43) chain C residue 422 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 44) chain C residue 235 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11513584 source Swiss-Prot : SWS_FT_FI3 45) chain C residue 266 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11513584 source Swiss-Prot : SWS_FT_FI3

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