eF-site ID 5gk6-B PDB Code 5gk6 Chain 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 B:  SKIFDFVKPGVITGDDVQKVFQVAKENNFALPAVNCVGTD SINAVLETAAKVKAPVIVQFSNGGASFIAGKGVKSDVPQG AAILGAISGAHHVHQMAEHYGVPVILHTDHCAKKLLPWID GLLDAGEKHFAATGKPLFSSHMIDLSEESLQENIEICSKY LERMSKIGMTLEIELGCLYTQPEDVDYAYTELSKISPRFT IAASFGNVLTPTILRDSQEYVSKKHNLPHNSLNFVFHGGS GSTAQEIKDSVSYGVVKMNIDTDTQWATWEGVLNYYKANE AYLQGQLGNPKGEDQPNKKYYDPRVWLRAGQTSMIARLEK AFQELNAIDVL Description Functional site 1) chain B residue 88 type sequence S description binding site for residue PEG A 403 source : AC3 2) chain B residue 91 type sequence H description binding site for residue PEG A 403 source : AC3 3) chain B residue 92 type sequence H description binding site for residue PEG A 403 source : AC3 4) chain B residue 95 type sequence Q description binding site for residue PEG A 403 source : AC3 5) chain B residue 110 type sequence H description binding site for residue ZN B 401 source : AC4 6) chain B residue 264 type sequence H description binding site for residue ZN B 401 source : AC4 7) chain B residue 110 type sequence H description binding site for residue CIT B 402 source : AC5 8) chain B residue 264 type sequence H description binding site for residue CIT B 402 source : AC5 9) chain B residue 265 type sequence G description binding site for residue CIT B 402 source : AC5 10) chain B residue 109 type catalytic sequence D description 52 source MCSA : MCSA2 11) chain B residue 110 type catalytic sequence H description 52 source MCSA : MCSA2 12) chain B residue 264 type catalytic sequence H description 52 source MCSA : MCSA2 13) chain B residue 286 type catalytic sequence N description 52 source MCSA : MCSA2 14) chain B residue 109 type ACT_SITE sequence D description Proton donor => ECO:0000269|PubMed:10080900 source Swiss-Prot : SWS_FT_FI1 15) chain B residue 61 type BINDING sequence S description BINDING => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 16) 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 17) 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 18) 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 19) 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 20) chain B residue 265 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI4 21) chain B residue 286 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI4 22) chain B residue 8 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI5 23) chain B residue 250 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI6 24) chain B residue 318 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI6 25) chain B residue 325 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI6 26) chain B residue 347 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI6 27) chain B residue 71 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI6 28) chain B residue 114 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI6

Display surface Download Links