eF-site ID 1ecq-ABCD PDB Code 1ecq Chain A, B, C, D click to enlarge Title E. COLI GLUCARATE DEHYDRATASE BOUND TO 4-DEOXYGLUCARATE Classification LYASE Compound GLUCARATE DEHYDRATASE Source (GUDH_ECOLI) Sequence A:  SQFTTPVVTEMQVIPVAGHDSMLMNLSGAHAPFFTRNIVI IKDNSGHTGVGEIPGGEKIRKTLEDAIPLVVGKTLGEYKN VLTLVRNTFADRDAGGRGLQTFDLRTTIHVVTGIEAAMLD LLGQHLGVNVASLLGDGQQRSEVEMLGYLFFVGNRKATPL PYQSQPDDSCDWYRLRHEEAMTPDAVVRLAEAAYEKYGFN DFKLKGGVLAGEEEAESIVALAQRFPQARITLDPNGAWSL NEAIKIGKYLKGSLAYAEDPCGAEQGFSGREVMAEFRRAT GLPTATNMIATDWRQMGHTLSLQSVDIPLADPHFWTMQGS VRVAQMCHEFGLTWGSHSNNHFDISLAMFTHVAAAAPGKI TAIDTHWIWQEGNQRLTKEPFEIKGGLVQVPEKPGLGVEI DMDQVMKAHELYQKHGLGARDDAMGMQYLIPGWTFDNKRP CMVR B:  FTTPVVTEMQVIPVAGHDSMLMNLSGAHAPFFTRNIVIIK DNSGHTGVGEIPGGEKIRKTLEDAIPLVVGKTLGEYKNVL TLVRNTFADRDAGGRGLQTFDLRTTIHVVTGIEAAMLDLL GQHLGVNVASLLGDGQQRSEVEMLGYLFFVGNRKATPLPY QSQPDDSCDWYRLRHEEAMTPDAVVRLAEAAYEKYGFNDF KLKGGVLAGEEEAESIVALAQRFPQARITLDPNGAWSLNE AIKIGKYLKGSLAYAEDPCGAEQGFSGREVMAEFRRATGL PTATNMIATDWRQMGHTLSLQSVDIPLADPHFWTMQGSVR VAQMCHEFGLTWGSHSNNHFDISLAMFTHVAAAAPGKITA IDTHWIWQEGNQRLTKEPFEIKGGLVQVPEKPGLGVEIDM DQVMKAHELYQKHGLGARDDAMGMQYLIPGWTFDNKRPCM VR C:  QFTTPVVTEMQVIPVAGHDSMLMNLSGAHAPFFTRNIVII KDNSGHTGVGEIPGGEKIRKTLEDAIPLVVGKTLGEYKNV LTLVRNTFADRDAGGRGLQTFDLRTTIHVVTGIEAAMLDL LGQHLGVNVASLLGDGQQRSEVEMLGYLFFVGNRKATPLP YQSQPDDSCDWYRLRHEEAMTPDAVVRLAEAAYEKYGFND FKLKGGVLAGEEEAESIVALAQRFPQARITLDPNGAWSLN EAIKIGKYLKGSLAYAEDPCGAEQGFSGREVMAEFRRATG LPTATNMIATDWRQMGHTLSLQSVDIPLADPHFWTMQGSV RVAQMCHEFGLTWGSHSNNHFDISLAMFTHVAAAAPGKIT AIDTHWIWQEGNQRLTKEPFEIKGGLVQVPEKPGLGVEID MDQVMKAHELYQKHGLGARDDAMGMQYLIPGWTFDNKRPC MVR D:  FTTPVVTEMQVIPVAGHDSMLMNLSGAHAPFFTRNIVIIK DNSGHTGVGEIPGGEKIRKTLEDAIPLVVGKTLGEYKNVL TLVRNTFADRDAGGRGLQTFDLRTTIHVVTGIEAAMLDLL GQHLGVNVASLLGDGQQRSEVEMLGYLFFVGNRKATPLPY QSQPDDSCDWYRLRHEEAMTPDAVVRLAEAAYEKYGFNDF KLKGGVLAGEEEAESIVALAQRFPQARITLDPNGAWSLNE AIKIGKYLKGSLAYAEDPCGAEQGFSGREVMAEFRRATGL PTATNMIATDWRQMGHTLSLQSVDIPLADPHFWTMQGSVR VAQMCHEFGLTWGSHSNNHFDISLAMFTHVAAAAPGKITA IDTHWIWQEGNQRLTKEPFEIKGGLVQVPEKPGLGVEIDM DQVMKAHELYQKHGLGARDDAMGMQYLIPGWTFDNKRPCM VR Description Functional site 1) chain A residue 27 type sequence N description BINDING SITE FOR RESIDUE DXG A 499 source : AC1 2) chain A residue 32 type sequence H description BINDING SITE FOR RESIDUE DXG A 499 source : AC1 3) chain A residue 103 type sequence T description BINDING SITE FOR RESIDUE DXG A 499 source : AC1 4) chain A residue 150 type sequence Y description BINDING SITE FOR RESIDUE DXG A 499 source : AC1 5) chain A residue 205 type sequence K description BINDING SITE FOR RESIDUE DXG A 499 source : AC1 6) chain A residue 207 type sequence K description BINDING SITE FOR RESIDUE DXG A 499 source : AC1 7) chain A residue 235 type sequence D description BINDING SITE FOR RESIDUE DXG A 499 source : AC1 8) chain A residue 237 type sequence N description BINDING SITE FOR RESIDUE DXG A 499 source : AC1 9) chain A residue 260 type sequence E description BINDING SITE FOR RESIDUE DXG A 499 source : AC1 10) chain A residue 289 type sequence N description BINDING SITE FOR RESIDUE DXG A 499 source : AC1 11) chain A residue 339 type sequence H description BINDING SITE FOR RESIDUE DXG A 499 source : AC1 12) chain A residue 340 type sequence S description BINDING SITE FOR RESIDUE DXG A 499 source : AC1 13) chain A residue 341 type sequence N description BINDING SITE FOR RESIDUE DXG A 499 source : AC1 14) chain A residue 368 type sequence H description BINDING SITE FOR RESIDUE DXG A 499 source : AC1 15) chain A residue 422 type sequence R description BINDING SITE FOR RESIDUE DXG A 499 source : AC1 16) chain B residue 27 type sequence N description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 17) chain B residue 32 type sequence H description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 18) chain B residue 103 type sequence T description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 19) chain B residue 150 type sequence Y description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 20) chain B residue 152 type sequence F description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 21) chain B residue 205 type sequence K description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 22) chain B residue 207 type sequence K description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 23) chain B residue 235 type sequence D description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 24) chain B residue 237 type sequence N description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 25) chain B residue 260 type sequence E description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 26) chain B residue 289 type sequence N description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 27) chain B residue 339 type sequence H description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 28) chain B residue 340 type sequence S description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 29) chain B residue 341 type sequence N description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 30) chain B residue 368 type sequence H description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 31) chain B residue 422 type sequence R description BINDING SITE FOR RESIDUE DXG B 500 source : AC2 32) chain C residue 27 type sequence N description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 33) chain C residue 32 type sequence H description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 34) chain C residue 103 type sequence T description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 35) chain C residue 104 type sequence F description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 36) chain C residue 150 type sequence Y description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 37) chain C residue 205 type sequence K description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 38) chain C residue 207 type sequence K description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 39) chain C residue 235 type sequence D description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 40) chain C residue 237 type sequence N description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 41) chain C residue 260 type sequence E description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 42) chain C residue 289 type sequence N description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 43) chain C residue 339 type sequence H description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 44) chain C residue 340 type sequence S description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 45) chain C residue 341 type sequence N description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 46) chain C residue 368 type sequence H description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 47) chain C residue 422 type sequence R description BINDING SITE FOR RESIDUE DXG C 501 source : AC3 48) chain D residue 27 type sequence N description BINDING SITE FOR RESIDUE DXG D 502 source : AC4 49) chain D residue 32 type sequence H description BINDING SITE FOR RESIDUE DXG D 502 source : AC4 50) chain D residue 103 type sequence T description BINDING SITE FOR RESIDUE DXG D 502 source : AC4 51) chain D residue 104 type sequence F description BINDING SITE FOR RESIDUE DXG D 502 source : AC4 52) chain D residue 150 type sequence Y description BINDING SITE FOR RESIDUE DXG D 502 source : AC4 53) chain D residue 152 type sequence F description BINDING SITE FOR RESIDUE DXG D 502 source : AC4 54) chain D residue 205 type sequence K description BINDING SITE FOR RESIDUE DXG D 502 source : AC4 55) chain D residue 207 type sequence K description BINDING SITE FOR RESIDUE DXG D 502 source : AC4 56) chain D residue 235 type sequence D description BINDING SITE FOR RESIDUE DXG D 502 source : AC4 57) chain D residue 237 type sequence N description BINDING SITE FOR RESIDUE DXG D 502 source : AC4 58) chain D residue 260 type sequence E description BINDING SITE FOR RESIDUE DXG D 502 source : AC4 59) chain D residue 289 type sequence N description BINDING SITE FOR RESIDUE DXG D 502 source : AC4 60) chain D residue 339 type sequence H description BINDING SITE FOR RESIDUE DXG D 502 source : AC4 61) chain D residue 340 type sequence S description BINDING SITE FOR RESIDUE DXG D 502 source : AC4 62) chain D residue 341 type sequence N description BINDING SITE FOR RESIDUE DXG D 502 source : AC4 63) chain D residue 366 type sequence D description BINDING SITE FOR RESIDUE DXG D 502 source : AC4 64) chain D residue 368 type sequence H description BINDING SITE FOR RESIDUE DXG D 502 source : AC4 65) chain D residue 422 type sequence R description BINDING SITE FOR RESIDUE DXG D 502 source : AC4 66) chain A residue 235 type sequence D description BINDING SITE FOR RESIDUE MG A 498 source : AC5 67) chain A residue 260 type sequence E description BINDING SITE FOR RESIDUE MG A 498 source : AC5 68) chain A residue 289 type sequence N description BINDING SITE FOR RESIDUE MG A 498 source : AC5 69) chain B residue 235 type sequence D description BINDING SITE FOR RESIDUE MG B 498 source : AC6 70) chain B residue 260 type sequence E description BINDING SITE FOR RESIDUE MG B 498 source : AC6 71) chain B residue 289 type sequence N description BINDING SITE FOR RESIDUE MG B 498 source : AC6 72) chain C residue 205 type sequence K description BINDING SITE FOR RESIDUE MG C 498 source : AC7 73) chain C residue 235 type sequence D description BINDING SITE FOR RESIDUE MG C 498 source : AC7 74) chain C residue 260 type sequence E description BINDING SITE FOR RESIDUE MG C 498 source : AC7 75) chain C residue 289 type sequence N description BINDING SITE FOR RESIDUE MG C 498 source : AC7 76) chain D residue 235 type sequence D description BINDING SITE FOR RESIDUE MG D 498 source : AC8 77) chain D residue 260 type sequence E description BINDING SITE FOR RESIDUE MG D 498 source : AC8 78) chain D residue 289 type sequence N description BINDING SITE FOR RESIDUE MG D 498 source : AC8 79) chain B residue 302 type sequence L description BINDING SITE FOR RESIDUE IPA D 601 source : AC9 80) chain D residue 299 type sequence G description BINDING SITE FOR RESIDUE IPA D 601 source : AC9 81) chain D residue 303 type sequence S description BINDING SITE FOR RESIDUE IPA D 601 source : AC9 82) chain A residue 302 type sequence L description BINDING SITE FOR RESIDUE IPA A 602 source : BC1 83) chain A residue 332 type sequence F description BINDING SITE FOR RESIDUE IPA A 602 source : BC1 84) chain C residue 299 type sequence G description BINDING SITE FOR RESIDUE IPA A 602 source : BC1 85) chain C residue 303 type sequence S description BINDING SITE FOR RESIDUE IPA A 602 source : BC1 86) chain B residue 299 type sequence G description BINDING SITE FOR RESIDUE IPA B 603 source : BC2 87) chain B residue 303 type sequence S description BINDING SITE FOR RESIDUE IPA B 603 source : BC2 88) chain D residue 302 type sequence L description BINDING SITE FOR RESIDUE IPA B 603 source : BC2 89) chain D residue 332 type sequence F description BINDING SITE FOR RESIDUE IPA B 603 source : BC2 90) chain A residue 299 type sequence G description BINDING SITE FOR RESIDUE IPA C 604 source : BC3 91) chain A residue 302 type sequence L description BINDING SITE FOR RESIDUE IPA C 604 source : BC3 92) chain A residue 303 type sequence S description BINDING SITE FOR RESIDUE IPA C 604 source : BC3 93) chain C residue 302 type sequence L description BINDING SITE FOR RESIDUE IPA C 604 source : BC3 94) chain C residue 332 type sequence F description BINDING SITE FOR RESIDUE IPA C 604 source : BC3 95) chain A residue 205 type catalytic sequence K description 451 source MCSA : MCSA1 96) chain A residue 207 type catalytic sequence K description 451 source MCSA : MCSA1 97) chain A residue 235 type catalytic sequence D description 451 source MCSA : MCSA1 98) chain A residue 237 type catalytic sequence N description 451 source MCSA : MCSA1 99) chain A residue 260 type catalytic sequence E description 451 source MCSA : MCSA1 100) chain A residue 289 type catalytic sequence N description 451 source MCSA : MCSA1 101) chain A residue 313 type catalytic sequence D description 451 source MCSA : MCSA1 102) chain A residue 339 type catalytic sequence H description 451 source MCSA : MCSA1 103) chain A residue 341 type catalytic sequence N description 451 source MCSA : MCSA1 104) chain B residue 205 type catalytic sequence K description 451 source MCSA : MCSA2 105) chain B residue 207 type catalytic sequence K description 451 source MCSA : MCSA2 106) chain B residue 235 type catalytic sequence D description 451 source MCSA : MCSA2 107) chain B residue 237 type catalytic sequence N description 451 source MCSA : MCSA2 108) chain B residue 260 type catalytic sequence E description 451 source MCSA : MCSA2 109) chain B residue 289 type catalytic sequence N description 451 source MCSA : MCSA2 110) chain B residue 313 type catalytic sequence D description 451 source MCSA : MCSA2 111) chain B residue 339 type catalytic sequence H description 451 source MCSA : MCSA2 112) chain B residue 341 type catalytic sequence N description 451 source MCSA : MCSA2 113) chain C residue 205 type catalytic sequence K description 451 source MCSA : MCSA3 114) chain C residue 207 type catalytic sequence K description 451 source MCSA : MCSA3 115) chain C residue 235 type catalytic sequence D description 451 source MCSA : MCSA3 116) chain C residue 237 type catalytic sequence N description 451 source MCSA : MCSA3 117) chain C residue 260 type catalytic sequence E description 451 source MCSA : MCSA3 118) chain C residue 289 type catalytic sequence N description 451 source MCSA : MCSA3 119) chain C residue 313 type catalytic sequence D description 451 source MCSA : MCSA3 120) chain C residue 339 type catalytic sequence H description 451 source MCSA : MCSA3 121) chain C residue 341 type catalytic sequence N description 451 source MCSA : MCSA3 122) chain D residue 205 type catalytic sequence K description 451 source MCSA : MCSA4 123) chain D residue 207 type catalytic sequence K description 451 source MCSA : MCSA4 124) chain D residue 235 type catalytic sequence D description 451 source MCSA : MCSA4 125) chain D residue 237 type catalytic sequence N description 451 source MCSA : MCSA4 126) chain D residue 260 type catalytic sequence E description 451 source MCSA : MCSA4 127) chain D residue 289 type catalytic sequence N description 451 source MCSA : MCSA4 128) chain D residue 313 type catalytic sequence D description 451 source MCSA : MCSA4 129) chain D residue 339 type catalytic sequence H description 451 source MCSA : MCSA4 130) chain D residue 341 type catalytic sequence N description 451 source MCSA : MCSA4 131) chain A residue 207 type ACT_SITE sequence K description Proton acceptor => ECO:0000269|PubMed:11513584 source Swiss-Prot : SWS_FT_FI1 132) chain A residue 339 type ACT_SITE sequence H description Proton acceptor => ECO:0000269|PubMed:11513584 source Swiss-Prot : SWS_FT_FI1 133) chain B residue 207 type ACT_SITE sequence K description Proton acceptor => ECO:0000269|PubMed:11513584 source Swiss-Prot : SWS_FT_FI1 134) chain B residue 339 type ACT_SITE sequence H description Proton acceptor => ECO:0000269|PubMed:11513584 source Swiss-Prot : SWS_FT_FI1 135) chain C residue 207 type ACT_SITE sequence K description Proton acceptor => ECO:0000269|PubMed:11513584 source Swiss-Prot : SWS_FT_FI1 136) chain C residue 339 type ACT_SITE sequence H description Proton acceptor => ECO:0000269|PubMed:11513584 source Swiss-Prot : SWS_FT_FI1 137) chain D residue 207 type ACT_SITE sequence K description Proton acceptor => ECO:0000269|PubMed:11513584 source Swiss-Prot : SWS_FT_FI1 138) chain D residue 339 type ACT_SITE sequence H description Proton acceptor => ECO:0000269|PubMed:11513584 source Swiss-Prot : SWS_FT_FI1 139) chain A residue 32 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 140) chain B residue 103 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 141) chain B residue 150 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 142) chain B residue 205 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 143) chain B residue 289 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 144) chain B residue 339 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 145) chain B residue 368 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 146) chain B residue 422 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 147) chain C residue 32 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 148) chain C residue 103 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 149) chain C residue 150 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 150) chain A residue 103 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 151) chain C residue 205 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 152) chain C residue 289 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 153) chain C residue 339 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 154) chain C residue 368 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 155) chain C residue 422 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 156) chain D residue 32 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 157) chain D residue 103 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 158) chain D residue 150 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 159) chain D residue 205 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 160) chain D residue 289 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 161) chain A residue 150 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 162) chain D residue 339 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 163) chain D residue 368 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 164) chain D residue 422 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 165) chain A residue 205 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 166) chain A residue 289 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI2 167) chain A residue 339 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 168) chain A residue 368 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 169) chain A residue 422 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 170) chain B residue 32 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 171) chain A residue 235 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11513584 source Swiss-Prot : SWS_FT_FI3 172) chain A residue 266 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11513584 source Swiss-Prot : SWS_FT_FI3 173) chain B residue 235 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11513584 source Swiss-Prot : SWS_FT_FI3 174) chain B residue 266 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11513584 source Swiss-Prot : SWS_FT_FI3 175) chain C residue 235 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11513584 source Swiss-Prot : SWS_FT_FI3 176) chain C residue 266 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11513584 source Swiss-Prot : SWS_FT_FI3 177) chain D residue 235 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11513584 source Swiss-Prot : SWS_FT_FI3 178) chain D residue 266 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11513584 source Swiss-Prot : SWS_FT_FI3

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