eF-site ID 4fua-A PDB Code 4fua Chain A click to enlarge Title L-FUCULOSE-1-PHOSPHATE ALDOLASE COMPLEX WITH PGH Classification LYASE (ALDEHYDE) Compound L-FUCULOSE-1-PHOSPHATE ALDOLASE Source Escherichia coli (strain K12) (FUCA_ECOLI) Sequence A:  MERNKLARQIIDTCLEMTRLGLNQGTAGNVSVRYQDGMLI TPTGIPYEKLTESHIVFIDGNGKHEEGKLPSSEWRFHMAA YQSRPDANAVVHNHAVHCTAVSILNRSIPAIHYMIAAAGG NSIPCAPYATFGTRELSEHVALALKNRKATLLQHHGLIAC EVNLEKALWLAHEVEVLAQLYLTTLAITDPVPVLSDEEIA VVLEKF Description (1)  L-FUCULOSE-1-PHOSPHATE ALDOLASE, BETA-MERCAPTOETHANOL, PHOSPHOGLYCOLOHYDROXAMIC ACID Functional site 1) chain A residue 73 type sequence E description THE ACTIVE CENTER IS DEFINED BY THE ZINC ION, THE FOUR ZINC COORDINATING RESIDUES AND TYR-1 13 FROM THE ADJACENT SUBUNIT. source : ACT 2) chain A residue 92 type sequence H description THE ACTIVE CENTER IS DEFINED BY THE ZINC ION, THE FOUR ZINC COORDINATING RESIDUES AND TYR-1 13 FROM THE ADJACENT SUBUNIT. source : ACT 3) chain A residue 94 type sequence H description THE ACTIVE CENTER IS DEFINED BY THE ZINC ION, THE FOUR ZINC COORDINATING RESIDUES AND TYR-1 13 FROM THE ADJACENT SUBUNIT. source : ACT 4) chain A residue 155 type sequence H description THE ACTIVE CENTER IS DEFINED BY THE ZINC ION, THE FOUR ZINC COORDINATING RESIDUES AND TYR-1 13 FROM THE ADJACENT SUBUNIT. source : ACT 5) chain A residue 113 type sequence Y description THE ACTIVE CENTER IS DEFINED BY THE ZINC ION, THE FOUR ZINC COORDINATING RESIDUES AND TYR-1 13 FROM THE ADJACENT SUBUNIT. source : ACT 6) chain A residue 71 type sequence S description BINDING SITE FOR THE SUBSTRATE PHOSPHATE GROUP. source : PBS 7) chain A residue 72 type sequence S description BINDING SITE FOR THE SUBSTRATE PHOSPHATE GROUP. source : PBS 8) chain A residue 29 type sequence N description BINDING SITE FOR THE SUBSTRATE PHOSPHATE GROUP. source : PBS 9) chain A residue 43 type sequence T description BINDING SITE FOR THE SUBSTRATE PHOSPHATE GROUP. source : PBS 10) chain A residue 44 type sequence G description BINDING SITE FOR THE SUBSTRATE PHOSPHATE GROUP. source : PBS 11) chain A residue 92 type sequence H description BINDING SITE FOR RESIDUE ZN A 216 source : AC1 12) chain A residue 94 type sequence H description BINDING SITE FOR RESIDUE ZN A 216 source : AC1 13) chain A residue 113 type sequence Y description BINDING SITE FOR RESIDUE ZN A 216 source : AC1 14) chain A residue 155 type sequence H description BINDING SITE FOR RESIDUE ZN A 216 source : AC1 15) chain A residue 146 type sequence N description BINDING SITE FOR RESIDUE SO4 A 300 source : AC2 16) chain A residue 147 type sequence R description BINDING SITE FOR RESIDUE SO4 A 300 source : AC2 17) chain A residue 147 type sequence R description BINDING SITE FOR RESIDUE SO4 A 300 source : AC2 18) chain A residue 14 type sequence C description BINDING SITE FOR RESIDUE BME A 301 source : AC3 19) chain A residue 45 type sequence I description BINDING SITE FOR RESIDUE BME A 301 source : AC3 20) chain A residue 26 type sequence T description BINDING SITE FOR RESIDUE PGH A 217 source : AC4 21) chain A residue 28 type sequence G description BINDING SITE FOR RESIDUE PGH A 217 source : AC4 22) chain A residue 29 type sequence N description BINDING SITE FOR RESIDUE PGH A 217 source : AC4 23) chain A residue 43 type sequence T description BINDING SITE FOR RESIDUE PGH A 217 source : AC4 24) chain A residue 44 type sequence G description BINDING SITE FOR RESIDUE PGH A 217 source : AC4 25) chain A residue 71 type sequence S description BINDING SITE FOR RESIDUE PGH A 217 source : AC4 26) chain A residue 72 type sequence S description BINDING SITE FOR RESIDUE PGH A 217 source : AC4 27) chain A residue 73 type sequence E description BINDING SITE FOR RESIDUE PGH A 217 source : AC4 28) chain A residue 92 type sequence H description BINDING SITE FOR RESIDUE PGH A 217 source : AC4 29) chain A residue 94 type sequence H description BINDING SITE FOR RESIDUE PGH A 217 source : AC4 30) chain A residue 113 type sequence Y description BINDING SITE FOR RESIDUE PGH A 217 source : AC4 31) chain A residue 155 type sequence H description BINDING SITE FOR RESIDUE PGH A 217 source : AC4 32) chain A residue 73 type catalytic sequence E description 72 source MCSA : MCSA1 33) chain A residue 92 type catalytic sequence H description 72 source MCSA : MCSA1 34) chain A residue 94 type catalytic sequence H description 72 source MCSA : MCSA1 35) chain A residue 113 type catalytic sequence Y description 72 source MCSA : MCSA1 36) chain A residue 155 type catalytic sequence H description 72 source MCSA : MCSA1 37) chain A 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 38) chain A 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 39) chain A residue 73 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289 source Swiss-Prot : SWS_FT_FI1 40) chain A 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 41) chain A 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 42) chain A 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 43) chain A residue 73 type BINDING sequence E 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 44) chain A 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 45) chain A 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 46) chain A 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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