eF-site ID 3t2c-A PDB Code 3t2c Chain A click to enlarge Title Fructose-1,6-bisphosphate aldolase/phosphatase from Thermoproteus neutrophilus, DHAP-bound form Classification LYASE, HYDROLASE Compound Fructose-1,6-bisphosphate aldolase/phosphatase Source Thermoproteus neutrophilus (strain DSM 2338 / JCM 9278 / V24Sta) (B1YAL1_THENV) Sequence A:  MRVTVSIIKADVGGFPGHAHVHPKMLEYAAAKLKEAQKRG VIIDYFVYNVGDDISLLMTHTKGEDNKDIHGLAWETFKEV TDQIAKRFKLYGAGQDLLKDAFSGNIRGMGPQVAEMEFEE RPSEPIIAFAADKTEPGAFNLPLYKMFADPFTTAGLVIDP SMHEGFIFEVLDVVEHKVYLLKTPEDAYSLLGLIGTTGRY IIRKVFRRADGAPAAANSVERLSLIAGRYVGKDDPVLLVR AQSGLPAVGEVLEAFAHPHLVHGWMRGSHAGPLMPARFIS VDPERRIAIGPKMTRFDGPPKVGALGFQLHEGYLEGGVDL FDDPAFDYVRQTAAQIADYIRRMGPFQPHRLPPEEMEYTA LPKILAKVKPYPADQYEKDRKKYIEAVVK Description Functional site 1) chain A residue 232 type sequence K description BINDING SITE FOR RESIDUE MG A 408 source : AC1 2) chain A residue 234 type sequence D description BINDING SITE FOR RESIDUE MG A 408 source : AC1 3) chain A residue 52 type sequence D description BINDING SITE FOR RESIDUE MG A 409 source : AC2 4) chain A residue 53 type sequence D description BINDING SITE FOR RESIDUE MG A 409 source : AC2 5) chain A residue 132 type sequence D description BINDING SITE FOR RESIDUE MG A 409 source : AC2 6) chain A residue 133 type sequence K description BINDING SITE FOR RESIDUE MG A 409 source : AC2 7) chain A residue 234 type sequence D description BINDING SITE FOR RESIDUE MG A 409 source : AC2 8) chain A residue 11 type sequence D description BINDING SITE FOR RESIDUE MG A 410 source : AC3 9) chain A residue 18 type sequence H description BINDING SITE FOR RESIDUE MG A 410 source : AC3 10) chain A residue 52 type sequence D description BINDING SITE FOR RESIDUE MG A 410 source : AC3 11) chain A residue 95 type sequence Q description BINDING SITE FOR RESIDUE MG A 410 source : AC3 12) chain A residue 11 type sequence D description BINDING SITE FOR RESIDUE 13P A 411 source : AC4 13) chain A residue 18 type sequence H description BINDING SITE FOR RESIDUE 13P A 411 source : AC4 14) chain A residue 52 type sequence D description BINDING SITE FOR RESIDUE 13P A 411 source : AC4 15) chain A residue 95 type sequence Q description BINDING SITE FOR RESIDUE 13P A 411 source : AC4 16) chain A residue 132 type sequence D description BINDING SITE FOR RESIDUE 13P A 411 source : AC4 17) chain A residue 133 type sequence K description BINDING SITE FOR RESIDUE 13P A 411 source : AC4 18) chain A residue 229 type sequence Y description BINDING SITE FOR RESIDUE 13P A 411 source : AC4 19) chain A residue 231 type sequence G description BINDING SITE FOR RESIDUE 13P A 411 source : AC4 20) chain A residue 232 type sequence K description BINDING SITE FOR RESIDUE 13P A 411 source : AC4 21) chain A residue 234 type sequence D description BINDING SITE FOR RESIDUE 13P A 411 source : AC4 22) chain A residue 264 type sequence W description BINDING SITE FOR RESIDUE 13P A 411 source : AC4 23) chain A residue 265 type sequence M description BINDING SITE FOR RESIDUE 13P A 411 source : AC4 24) chain A residue 266 type sequence R description BINDING SITE FOR RESIDUE 13P A 411 source : AC4 25) chain A residue 267 type sequence G description BINDING SITE FOR RESIDUE 13P A 411 source : AC4 26) chain A residue 297 type sequence D description BINDING SITE FOR RESIDUE 13P A 411 source : AC4 27) chain A residue 18 type sequence H description BINDING SITE FOR RESIDUE 13P A 412 source : AC5 28) chain A residue 91 type sequence Y description BINDING SITE FOR RESIDUE 13P A 412 source : AC5 29) chain A residue 229 type sequence Y description BINDING SITE FOR RESIDUE 13P A 412 source : AC5 30) chain A residue 232 type sequence K description BINDING SITE FOR RESIDUE 13P A 412 source : AC5 31) chain A residue 242 type sequence Q description BINDING SITE FOR RESIDUE 13P A 412 source : AC5 32) chain A residue 243 type sequence S description BINDING SITE FOR RESIDUE 13P A 412 source : AC5 33) chain A residue 247 type sequence A description BINDING SITE FOR RESIDUE 13P A 412 source : AC5 34) chain A residue 266 type sequence R description BINDING SITE FOR RESIDUE 13P A 412 source : AC5 35) chain A residue 297 type sequence D description BINDING SITE FOR RESIDUE 13P A 412 source : AC5 36) chain A residue 358 type sequence Y description BINDING SITE FOR RESIDUE 13P A 412 source : AC5 37) chain A residue 11 type ACT_SITE sequence D description Proton acceptor; for FBP phosphatase activity => ECO:0000250|UniProtKB:F9VMT6 source Swiss-Prot : SWS_FT_FI1 38) chain A residue 229 type ACT_SITE sequence Y description Proton donor/acceptor; for FBP aldolase activity => ECO:0000305|PubMed:21983965 source Swiss-Prot : SWS_FT_FI2 39) chain A residue 232 type ACT_SITE sequence K description Schiff-base intermediate with DHAP; for FBP aldolase activity => ECO:0000269|PubMed:21983965 source Swiss-Prot : SWS_FT_FI3 40) chain A residue 11 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21983965, ECO:0007744|PDB:3T2B, ECO:0007744|PDB:3T2C, ECO:0007744|PDB:3T2D source Swiss-Prot : SWS_FT_FI4 41) chain A residue 18 type BINDING sequence H description BINDING => ECO:0000269|PubMed:21983965, ECO:0007744|PDB:3T2B, ECO:0007744|PDB:3T2C, ECO:0007744|PDB:3T2D source Swiss-Prot : SWS_FT_FI4 42) chain A residue 52 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21983965, ECO:0007744|PDB:3T2B, ECO:0007744|PDB:3T2C, ECO:0007744|PDB:3T2D source Swiss-Prot : SWS_FT_FI4 43) chain A residue 53 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21983965, ECO:0007744|PDB:3T2B, ECO:0007744|PDB:3T2C, ECO:0007744|PDB:3T2D source Swiss-Prot : SWS_FT_FI4 44) chain A residue 132 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21983965, ECO:0007744|PDB:3T2B, ECO:0007744|PDB:3T2C, ECO:0007744|PDB:3T2D source Swiss-Prot : SWS_FT_FI4 45) chain A residue 91 type BINDING sequence Y description in other chain => ECO:0000269|PubMed:21983965, ECO:0007744|PDB:3T2D source Swiss-Prot : SWS_FT_FI5 46) chain A residue 104 type BINDING sequence G description in other chain => ECO:0000269|PubMed:21983965, ECO:0007744|PDB:3T2D source Swiss-Prot : SWS_FT_FI5 47) chain A residue 358 type BINDING sequence Y description in other chain => ECO:0000269|PubMed:21983965, ECO:0007744|PDB:3T2D source Swiss-Prot : SWS_FT_FI5 48) chain A residue 95 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:21983965, ECO:0007744|PDB:3T2C, ECO:0007744|PDB:3T2D, ECO:0007744|PDB:3T2E source Swiss-Prot : SWS_FT_FI6 49) chain A residue 133 type BINDING sequence K description BINDING => ECO:0000269|PubMed:21983965, ECO:0007744|PDB:3T2C source Swiss-Prot : SWS_FT_FI7 50) chain A residue 266 type BINDING sequence R description BINDING => ECO:0000269|PubMed:21983965, ECO:0007744|PDB:3T2C source Swiss-Prot : SWS_FT_FI7 51) chain A residue 297 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21983965, ECO:0007744|PDB:3T2C source Swiss-Prot : SWS_FT_FI7 52) chain A residue 232 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:F9VMT6 source Swiss-Prot : SWS_FT_FI8 53) chain A residue 233 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21983965 source Swiss-Prot : SWS_FT_FI9 54) chain A residue 234 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21983965 source Swiss-Prot : SWS_FT_FI9 55) chain A residue 242 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:21983965 source Swiss-Prot : SWS_FT_FI9

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