eF-site ID 5gk6-AB PDB Code 5gk6 Chain A, B click to enlarge Title Structure of E.Coli fructose 1,6-bisphosphate aldolase, Citrate bound form Classification LYASE Compound Fructose-bisphosphate aldolase class 2 Source Escherichia coli (strain K12) (ALF_ECOLI) Sequence A:  SKIFDFVKPGVITGDDVQKVFQVAKENNFALPAVNCVGTD SINAVLETAAKVKAPVIVQFSNGGASFIAGKGVKSDVPQG AAILGAISGAHHVHQMAEHYGVPVILHTDHCAKKLLPWID GLLDAGEKHFAATGKPLFSSHMIDLSEESLQENIEICSKY LERMSKIGMTLEIELGCTLYTQPEDVDYAYTELSKISPRF TIAASFGNVVLTPTILRDSQEYVSKKHNLPHNSLNFVFHG GSGSTAQEIKDSVSYGVVKMNIDTDTQWATWEGVLNYYKA NEAYLQGQLGNPKGEDQPNKKYYDPRVWLRAGQTSMIARL EKAFQELNAIDVL B:  SKIFDFVKPGVITGDDVQKVFQVAKENNFALPAVNCVGTD SINAVLETAAKVKAPVIVQFSNGGASFIAGKGVKSDVPQG AAILGAISGAHHVHQMAEHYGVPVILHTDHCAKKLLPWID GLLDAGEKHFAATGKPLFSSHMIDLSEESLQENIEICSKY LERMSKIGMTLEIELGCLYTQPEDVDYAYTELSKISPRFT IAASFGNVLTPTILRDSQEYVSKKHNLPHNSLNFVFHGGS GSTAQEIKDSVSYGVVKMNIDTDTQWATWEGVLNYYKANE AYLQGQLGNPKGEDQPNKKYYDPRVWLRAGQTSMIARLEK AFQELNAIDVL Description Functional site 1) chain A residue 110 type sequence H description binding site for residue ZN A 401 source : AC1 2) chain A residue 264 type sequence H description binding site for residue ZN A 401 source : AC1 3) chain A residue 110 type sequence H description binding site for residue CIT A 402 source : AC2 4) chain A residue 264 type sequence H description binding site for residue CIT A 402 source : AC2 5) chain A residue 265 type sequence G description binding site for residue CIT A 402 source : AC2 6) chain A residue 88 type sequence S description binding site for residue PEG A 403 source : AC3 7) chain A residue 91 type sequence H description binding site for residue PEG A 403 source : AC3 8) chain A residue 92 type sequence H description binding site for residue PEG A 403 source : AC3 9) chain B residue 88 type sequence S description binding site for residue PEG A 403 source : AC3 10) chain B residue 91 type sequence H description binding site for residue PEG A 403 source : AC3 11) chain B residue 92 type sequence H description binding site for residue PEG A 403 source : AC3 12) chain B residue 95 type sequence Q description binding site for residue PEG A 403 source : AC3 13) chain B residue 110 type sequence H description binding site for residue ZN B 401 source : AC4 14) chain B residue 264 type sequence H description binding site for residue ZN B 401 source : AC4 15) chain B residue 110 type sequence H description binding site for residue CIT B 402 source : AC5 16) chain B residue 264 type sequence H description binding site for residue CIT B 402 source : AC5 17) chain B residue 265 type sequence G description binding site for residue CIT B 402 source : AC5 18) chain A residue 109 type catalytic sequence D description 52 source MCSA : MCSA1 19) chain A residue 110 type catalytic sequence H description 52 source MCSA : MCSA1 20) chain A residue 264 type catalytic sequence H description 52 source MCSA : MCSA1 21) chain A residue 286 type catalytic sequence N description 52 source MCSA : MCSA1 22) chain B residue 109 type catalytic sequence D description 52 source MCSA : MCSA2 23) chain B residue 110 type catalytic sequence H description 52 source MCSA : MCSA2 24) chain B residue 264 type catalytic sequence H description 52 source MCSA : MCSA2 25) chain B residue 286 type catalytic sequence N description 52 source MCSA : MCSA2 26) chain A residue 100-111 type prosite sequence YGVPVILHTDHC description ALDOLASE_CLASS_II_1 Fructose-bisphosphate aldolase class-II signature 1. Yg..VPVi.LHtDHC source prosite : PS00602 27) chain A residue 109 type ACT_SITE sequence D description Proton donor => ECO:0000269|PubMed:10080900 source Swiss-Prot : SWS_FT_FI1 28) chain B residue 109 type ACT_SITE sequence D description Proton donor => ECO:0000269|PubMed:10080900 source Swiss-Prot : SWS_FT_FI1 29) chain A residue 61 type BINDING sequence S description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 30) chain B residue 61 type BINDING sequence S description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 31) chain A residue 110 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10080900, ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754 source Swiss-Prot : SWS_FT_FI3 32) chain B residue 264 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10080900, ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754 source Swiss-Prot : SWS_FT_FI3 33) chain A residue 144 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10080900, ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754 source Swiss-Prot : SWS_FT_FI3 34) chain A residue 174 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10080900, ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754 source Swiss-Prot : SWS_FT_FI3 35) chain A residue 264 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10080900, ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754 source Swiss-Prot : SWS_FT_FI3 36) chain B residue 110 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10080900, ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754 source Swiss-Prot : SWS_FT_FI3 37) chain B residue 144 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10080900, ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754 source Swiss-Prot : SWS_FT_FI3 38) chain B residue 174 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10080900, ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754 source Swiss-Prot : SWS_FT_FI3 39) chain A residue 265 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI4 40) chain A residue 286 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI4 41) chain B residue 265 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI4 42) chain B residue 286 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI4 43) chain A residue 8 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI5 44) chain B residue 8 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI5 45) chain A residue 71 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI6 46) chain B residue 250 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI6 47) chain B residue 318 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI6 48) chain B residue 325 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI6 49) chain B residue 347 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI6 50) chain A residue 114 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI6 51) chain A residue 250 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI6 52) chain A residue 318 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI6 53) chain A residue 325 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI6 54) chain A residue 347 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI6 55) chain B residue 71 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI6 56) chain B residue 114 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI6

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