eF-site ID 1e46-P PDB Code 1e46 Chain P click to enlarge Title L-Fuculose 1-Phosphate Aldolase from Escherichia coli Mutant E73S Classification ALDOLASE (CLASS II) Compound L-FUCULOSE 1-PHOSPHATE ALDOLASE Source (FUCA_ECOLI) Sequence P:  MERNKLARQIIDTCLEMTRLGLNQGTAGNVSVRYQDGMLI TPTGIPYEKLTESHIVFIDGNGKHEEGKLPSSSWRFHMAA YQSRPDANAVVHNHAVHCTAVSILNRSIPAIHYMIAAAGG NSIPCAPYATFGTRELSEHVALALKNRKATLLQHHGLIAC EVNLEKALWLAHEVEVLAQLYLTTLAITDPVPVLSDEEIA VVLEKF Description (1)  L-FUCULOSE 1-PHOSPHATE ALDOLASE (E.C.4.1.2.17) Functional site 1) chain P residue 29 type sequence N description BINDING SITE FOR RESIDUE SO4 S 300 source : AC1 2) chain P residue 43 type sequence T description BINDING SITE FOR RESIDUE SO4 S 300 source : AC1 3) chain P residue 71 type sequence S description BINDING SITE FOR RESIDUE SO4 S 300 source : AC1 4) chain P residue 72 type sequence S description BINDING SITE FOR RESIDUE SO4 S 300 source : AC1 5) chain P residue 92 type sequence H description BINDING SITE FOR RESIDUE ZN S 999 source : AC2 6) chain P residue 94 type sequence H description BINDING SITE FOR RESIDUE ZN S 999 source : AC2 7) chain P residue 155 type sequence H description BINDING SITE FOR RESIDUE ZN S 999 source : AC2 8) chain P residue 14 type sequence C description BINDING SITE FOR RESIDUE BME S 314 source : AC3 9) chain P residue 26 type sequence T description BINDING SITE FOR RESIDUE BME S 314 source : AC3 10) chain P residue 28 type sequence G description BINDING SITE FOR RESIDUE BME S 314 source : AC3 11) chain P residue 41 type sequence T description BINDING SITE FOR RESIDUE BME S 314 source : AC3 12) chain P residue 73 type catalytic sequence S description 72 source MCSA : MCSA1 13) chain P residue 92 type catalytic sequence H description 72 source MCSA : MCSA1 14) chain P residue 94 type catalytic sequence H description 72 source MCSA : MCSA1 15) chain P residue 113 type catalytic sequence Y description 72 source MCSA : MCSA1 16) chain P residue 155 type catalytic sequence H description 72 source MCSA : MCSA1 17) chain P residue 73 type ACT_SITE sequence S description Proton donor/acceptor => ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289 source Swiss-Prot : SWS_FT_FI1 18) chain P residue 28 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:8676381, ECO:0007744|PDB:1E47, ECO:0007744|PDB:1E48, ECO:0007744|PDB:4FUA source Swiss-Prot : SWS_FT_FI2 19) chain P residue 43 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:8676381, ECO:0007744|PDB:1E47, ECO:0007744|PDB:1E48, ECO:0007744|PDB:4FUA source Swiss-Prot : SWS_FT_FI2 20) chain P residue 71 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:8676381, ECO:0007744|PDB:1E47, ECO:0007744|PDB:1E48, ECO:0007744|PDB:4FUA source Swiss-Prot : SWS_FT_FI2 21) chain P residue 73 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:15299567, ECO:0000269|PubMed:8676381, ECO:0007744|PDB:1DZU, ECO:0007744|PDB:1DZV, ECO:0007744|PDB:1DZW, ECO:0007744|PDB:1DZX, ECO:0007744|PDB:1DZY, ECO:0007744|PDB:1DZZ, ECO:0007744|PDB:1E48, ECO:0007744|PDB:1E49, ECO:0007744|PDB:1E4A, ECO:0007744|PDB:1E4B, ECO:0007744|PDB:1E4C, ECO:0007744|PDB:1FUA, ECO:0007744|PDB:2FUA, ECO:0007744|PDB:3FUA, ECO:0007744|PDB:4FUA source Swiss-Prot : SWS_FT_FI3 22) chain P residue 113 type SITE sequence Y description Plays a key role in the stabilization of the transition state and positioning the aldehyde component => ECO:0000269|PubMed:10821675 source Swiss-Prot : SWS_FT_FI5 23) chain P residue 131 type SITE sequence F description Plays a key role in the stabilization of the transition state and positioning the aldehyde component => ECO:0000269|PubMed:10821675 source Swiss-Prot : SWS_FT_FI5 24) chain P residue 92 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:15299567, ECO:0000269|PubMed:8676381, ECO:0007744|PDB:1DZU, ECO:0007744|PDB:1DZV, ECO:0007744|PDB:1DZW, ECO:0007744|PDB:1DZX, ECO:0007744|PDB:1DZY, ECO:0007744|PDB:1DZZ, ECO:0007744|PDB:1E46, ECO:0007744|PDB:1E47, ECO:0007744|PDB:1E48, ECO:0007744|PDB:1E49, ECO:0007744|PDB:1E4A, ECO:0007744|PDB:1E4B, ECO:0007744|PDB:1E4C, ECO:0007744|PDB:1FUA, ECO:0007744|PDB:2FUA, ECO:0007744|PDB:3FUA, ECO:0007744|PDB:4FUA source Swiss-Prot : SWS_FT_FI4 25) chain P residue 94 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:15299567, ECO:0000269|PubMed:8676381, ECO:0007744|PDB:1DZU, ECO:0007744|PDB:1DZV, ECO:0007744|PDB:1DZW, ECO:0007744|PDB:1DZX, ECO:0007744|PDB:1DZY, ECO:0007744|PDB:1DZZ, ECO:0007744|PDB:1E46, ECO:0007744|PDB:1E47, ECO:0007744|PDB:1E48, ECO:0007744|PDB:1E49, ECO:0007744|PDB:1E4A, ECO:0007744|PDB:1E4B, ECO:0007744|PDB:1E4C, ECO:0007744|PDB:1FUA, ECO:0007744|PDB:2FUA, ECO:0007744|PDB:3FUA, ECO:0007744|PDB:4FUA source Swiss-Prot : SWS_FT_FI4 26) chain P residue 155 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:15299567, ECO:0000269|PubMed:8676381, ECO:0007744|PDB:1DZU, ECO:0007744|PDB:1DZV, ECO:0007744|PDB:1DZW, ECO:0007744|PDB:1DZX, ECO:0007744|PDB:1DZY, ECO:0007744|PDB:1DZZ, ECO:0007744|PDB:1E46, ECO:0007744|PDB:1E47, ECO:0007744|PDB:1E48, ECO:0007744|PDB:1E49, ECO:0007744|PDB:1E4A, ECO:0007744|PDB:1E4B, ECO:0007744|PDB:1E4C, ECO:0007744|PDB:1FUA, ECO:0007744|PDB:2FUA, ECO:0007744|PDB:3FUA, ECO:0007744|PDB:4FUA source Swiss-Prot : SWS_FT_FI4

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