eF-site ID 1og6-ABC PDB Code 1og6 Chain A, B, C click to enlarge Title ydhF, an aldo-keto reductase from E.coli complexed with NADPH Classification OXIDOREDUCTASE Compound HYPOTHETICAL OXIDOREDUCTASE YDHF Source null (YDHF_ECOLI) Sequence A:  LVQRITIAPQGPEFSRFVMGYWRLMDWNMSARQLVSFIEE HLDLGVTTVDHADIYGGYQCEAAFGEALKLAPHLRERMEI VSKCGIATTAREENVIGHYITDRDHIIKSAEQSLINLATD HLDLLLIHRPDPLMDADEVADAFKHLHQSGKVRHFGVSNF TPAQFALLQSRLPFTLATNQVEISPVHQPLLLDGTLDQLQ QLRVRPMAWSCLGGGRLFNDDYFQPLRDELAVVAEELNAG SIEQVVNAWVLRLPSQPLPIIGSGKIERVRAAVEAETLKM TRQQWFRIRKAALGYDVP B:  LVQRITIAPQGPEFSRFVMGYWRLMDWNMSARQLVSFIEE HLDLGVTTVDHADIYGGYQCEAAFGEALKLAPHLRERMEI VSKCGIATTAREENVIGHYITDRDHIIKSAEQSLINLATD HLDLLLIHRPDPLMDADEVADAFKHLHQSGKVRHFGVSNF TPAQFALLQSRLPFTLATNQVEISPVHQPLLLDGTLDQLQ QLRVRPMAWSCRLFNDDYFQPLRDELAVVAEELNAGSIEQ VVNAWVLRLPSQPLPIIGSGKIERVRAAVEAETLKMTRQQ WFRIRKAALGYDVP C:  LVQRITIAPQGPEFSRFVMGYWRLMDWNMSARQLVSFIEE HLDLGVTTVDHADIYGGYQCEAAFGEALKLAPHLRERMEI VSKCGIATTAREENVIGHYITDRDHIIKSAEQSLINLATD HLDLLLIHRPDPLMDADEVADAFKHLHQSGKVRHFGVSNF TPAQFALLQSRLPFTLATNQVEISPVHQPLLLDGTLDQLQ QLRVRPMAWSCLGGGRLFNDDYFQPLRDELAVVAEELNAG SIEQVVNAWVLRLPSQPLPIIGSGKIERVRAAVEAETLKM TRQQWFRIRKAALGYDVP Description (1)  HYPOTHETICAL OXIDOREDUCTASE YDHF Functional site 1) chain A residue 20 type sequence G description BINDING SITE FOR RESIDUE NAP A1298 source : AC1 2) chain A residue 22 type sequence W description BINDING SITE FOR RESIDUE NAP A1298 source : AC1 3) chain A residue 23 type sequence R description BINDING SITE FOR RESIDUE NAP A1298 source : AC1 4) chain A residue 50 type sequence D description BINDING SITE FOR RESIDUE NAP A1298 source : AC1 5) chain A residue 55 type sequence Y description BINDING SITE FOR RESIDUE NAP A1298 source : AC1 6) chain A residue 128 type sequence H description BINDING SITE FOR RESIDUE NAP A1298 source : AC1 7) chain A residue 129 type sequence R description BINDING SITE FOR RESIDUE NAP A1298 source : AC1 8) chain A residue 158 type sequence S description BINDING SITE FOR RESIDUE NAP A1298 source : AC1 9) chain A residue 159 type sequence N description BINDING SITE FOR RESIDUE NAP A1298 source : AC1 10) chain A residue 180 type sequence Q description BINDING SITE FOR RESIDUE NAP A1298 source : AC1 11) chain A residue 209 type sequence W description BINDING SITE FOR RESIDUE NAP A1298 source : AC1 12) chain A residue 210 type sequence S description BINDING SITE FOR RESIDUE NAP A1298 source : AC1 13) chain A residue 212 type sequence L description BINDING SITE FOR RESIDUE NAP A1298 source : AC1 14) chain A residue 213 type sequence G description BINDING SITE FOR RESIDUE NAP A1298 source : AC1 15) chain A residue 214 type sequence G description BINDING SITE FOR RESIDUE NAP A1298 source : AC1 16) chain A residue 215 type sequence G description BINDING SITE FOR RESIDUE NAP A1298 source : AC1 17) chain A residue 218 type sequence F description BINDING SITE FOR RESIDUE NAP A1298 source : AC1 18) chain A residue 243 type sequence E description BINDING SITE FOR RESIDUE NAP A1298 source : AC1 19) chain A residue 260 type sequence I description BINDING SITE FOR RESIDUE NAP A1298 source : AC1 20) chain A residue 262 type sequence G description BINDING SITE FOR RESIDUE NAP A1298 source : AC1 21) chain A residue 263 type sequence S description BINDING SITE FOR RESIDUE NAP A1298 source : AC1 22) chain A residue 264 type sequence G description BINDING SITE FOR RESIDUE NAP A1298 source : AC1 23) chain A residue 265 type sequence K description BINDING SITE FOR RESIDUE NAP A1298 source : AC1 24) chain A residue 268 type sequence R description BINDING SITE FOR RESIDUE NAP A1298 source : AC1 25) chain B residue 20 type sequence G description BINDING SITE FOR RESIDUE NAP B1299 source : AC2 26) chain B residue 22 type sequence W description BINDING SITE FOR RESIDUE NAP B1299 source : AC2 27) chain B residue 23 type sequence R description BINDING SITE FOR RESIDUE NAP B1299 source : AC2 28) chain B residue 50 type sequence D description BINDING SITE FOR RESIDUE NAP B1299 source : AC2 29) chain B residue 55 type sequence Y description BINDING SITE FOR RESIDUE NAP B1299 source : AC2 30) chain B residue 128 type sequence H description BINDING SITE FOR RESIDUE NAP B1299 source : AC2 31) chain B residue 129 type sequence R description BINDING SITE FOR RESIDUE NAP B1299 source : AC2 32) chain B residue 158 type sequence S description BINDING SITE FOR RESIDUE NAP B1299 source : AC2 33) chain B residue 159 type sequence N description BINDING SITE FOR RESIDUE NAP B1299 source : AC2 34) chain B residue 180 type sequence Q description BINDING SITE FOR RESIDUE NAP B1299 source : AC2 35) chain B residue 209 type sequence W description BINDING SITE FOR RESIDUE NAP B1299 source : AC2 36) chain B residue 210 type sequence S description BINDING SITE FOR RESIDUE NAP B1299 source : AC2 37) chain B residue 218 type sequence F description BINDING SITE FOR RESIDUE NAP B1299 source : AC2 38) chain B residue 260 type sequence I description BINDING SITE FOR RESIDUE NAP B1299 source : AC2 39) chain B residue 262 type sequence G description BINDING SITE FOR RESIDUE NAP B1299 source : AC2 40) chain B residue 263 type sequence S description BINDING SITE FOR RESIDUE NAP B1299 source : AC2 41) chain B residue 264 type sequence G description BINDING SITE FOR RESIDUE NAP B1299 source : AC2 42) chain B residue 265 type sequence K description BINDING SITE FOR RESIDUE NAP B1299 source : AC2 43) chain B residue 268 type sequence R description BINDING SITE FOR RESIDUE NAP B1299 source : AC2 44) chain C residue 222 type sequence Y description BINDING SITE FOR RESIDUE NAP B1299 source : AC2 45) chain C residue 20 type sequence G description BINDING SITE FOR RESIDUE NAP C1299 source : AC3 46) chain C residue 22 type sequence W description BINDING SITE FOR RESIDUE NAP C1299 source : AC3 47) chain C residue 23 type sequence R description BINDING SITE FOR RESIDUE NAP C1299 source : AC3 48) chain C residue 50 type sequence D description BINDING SITE FOR RESIDUE NAP C1299 source : AC3 49) chain C residue 55 type sequence Y description BINDING SITE FOR RESIDUE NAP C1299 source : AC3 50) chain C residue 128 type sequence H description BINDING SITE FOR RESIDUE NAP C1299 source : AC3 51) chain C residue 129 type sequence R description BINDING SITE FOR RESIDUE NAP C1299 source : AC3 52) chain C residue 158 type sequence S description BINDING SITE FOR RESIDUE NAP C1299 source : AC3 53) chain C residue 159 type sequence N description BINDING SITE FOR RESIDUE NAP C1299 source : AC3 54) chain C residue 180 type sequence Q description BINDING SITE FOR RESIDUE NAP C1299 source : AC3 55) chain C residue 209 type sequence W description BINDING SITE FOR RESIDUE NAP C1299 source : AC3 56) chain C residue 210 type sequence S description BINDING SITE FOR RESIDUE NAP C1299 source : AC3 57) chain C residue 212 type sequence L description BINDING SITE FOR RESIDUE NAP C1299 source : AC3 58) chain C residue 213 type sequence G description BINDING SITE FOR RESIDUE NAP C1299 source : AC3 59) chain C residue 214 type sequence G description BINDING SITE FOR RESIDUE NAP C1299 source : AC3 60) chain C residue 215 type sequence G description BINDING SITE FOR RESIDUE NAP C1299 source : AC3 61) chain C residue 218 type sequence F description BINDING SITE FOR RESIDUE NAP C1299 source : AC3 62) chain C residue 243 type sequence E description BINDING SITE FOR RESIDUE NAP C1299 source : AC3 63) chain C residue 260 type sequence I description BINDING SITE FOR RESIDUE NAP C1299 source : AC3 64) chain C residue 262 type sequence G description BINDING SITE FOR RESIDUE NAP C1299 source : AC3 65) chain C residue 263 type sequence S description BINDING SITE FOR RESIDUE NAP C1299 source : AC3 66) chain C residue 264 type sequence G description BINDING SITE FOR RESIDUE NAP C1299 source : AC3 67) chain C residue 265 type sequence K description BINDING SITE FOR RESIDUE NAP C1299 source : AC3 68) chain C residue 268 type sequence R description BINDING SITE FOR RESIDUE NAP C1299 source : AC3 69) chain A residue 55 type ACT_SITE sequence Y description Proton donor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 70) chain B residue 55 type ACT_SITE sequence Y description Proton donor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 71) chain C residue 55 type ACT_SITE sequence Y description Proton donor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 72) chain A residue 158 type BINDING sequence S description BINDING => ECO:0000269|PubMed:14649299 source Swiss-Prot : SWS_FT_FI2 73) chain A residue 209 type BINDING sequence W description BINDING => ECO:0000269|PubMed:14649299 source Swiss-Prot : SWS_FT_FI2 74) chain A residue 263 type BINDING sequence S description BINDING => ECO:0000269|PubMed:14649299 source Swiss-Prot : SWS_FT_FI2 75) chain B residue 158 type BINDING sequence S description BINDING => ECO:0000269|PubMed:14649299 source Swiss-Prot : SWS_FT_FI2 76) chain B residue 209 type BINDING sequence W description BINDING => ECO:0000269|PubMed:14649299 source Swiss-Prot : SWS_FT_FI2 77) chain B residue 263 type BINDING sequence S description BINDING => ECO:0000269|PubMed:14649299 source Swiss-Prot : SWS_FT_FI2 78) chain C residue 158 type BINDING sequence S description BINDING => ECO:0000269|PubMed:14649299 source Swiss-Prot : SWS_FT_FI2 79) chain C residue 209 type BINDING sequence W description BINDING => ECO:0000269|PubMed:14649299 source Swiss-Prot : SWS_FT_FI2 80) chain C residue 263 type BINDING sequence S description BINDING => ECO:0000269|PubMed:14649299 source Swiss-Prot : SWS_FT_FI2

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