eF-site ID 3bcj-A PDB Code 3bcj Chain A click to enlarge Title Crystal structure of Aldose Reductase complexed with 2S4R (Stereoisomer of Fidarestat, 2S4S) at 0.78 A Classification OXIDOREDUCTASE Compound Aldose reductase Source Homo sapiens (Human) (ALDR_HUMAN) Sequence A:  MASRILLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGY RHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLW CTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGK EFFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGIS NFNHLQVEMILNKPGLKYKPAVNQIECHPYLTQEKLIQYC QSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAK HNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFE LSSQDMTTLLSYNRNWRVCALLSCTSHKDYPFHEEF Description Functional site 1) chain A residue 18 type sequence G description BINDING SITE FOR RESIDUE NAP A 318 source : AC1 2) chain A residue 19 type sequence T description BINDING SITE FOR RESIDUE NAP A 318 source : AC1 3) chain A residue 20 type sequence W description BINDING SITE FOR RESIDUE NAP A 318 source : AC1 4) chain A residue 21 type sequence K description BINDING SITE FOR RESIDUE NAP A 318 source : AC1 5) chain A residue 43 type sequence D description BINDING SITE FOR RESIDUE NAP A 318 source : AC1 6) chain A residue 48 type sequence Y description BINDING SITE FOR RESIDUE NAP A 318 source : AC1 7) chain A residue 110 type sequence H description BINDING SITE FOR RESIDUE NAP A 318 source : AC1 8) chain A residue 159 type sequence S description BINDING SITE FOR RESIDUE NAP A 318 source : AC1 9) chain A residue 160 type sequence N description BINDING SITE FOR RESIDUE NAP A 318 source : AC1 10) chain A residue 183 type sequence Q description BINDING SITE FOR RESIDUE NAP A 318 source : AC1 11) chain A residue 209 type sequence Y description BINDING SITE FOR RESIDUE NAP A 318 source : AC1 12) chain A residue 210 type sequence S description BINDING SITE FOR RESIDUE NAP A 318 source : AC1 13) chain A residue 211 type sequence P description BINDING SITE FOR RESIDUE NAP A 318 source : AC1 14) chain A residue 212 type sequence L description BINDING SITE FOR RESIDUE NAP A 318 source : AC1 15) chain A residue 213 type sequence G description BINDING SITE FOR RESIDUE NAP A 318 source : AC1 16) chain A residue 214 type sequence S description BINDING SITE FOR RESIDUE NAP A 318 source : AC1 17) chain A residue 215 type sequence P description BINDING SITE FOR RESIDUE NAP A 318 source : AC1 18) chain A residue 216 type sequence D description BINDING SITE FOR RESIDUE NAP A 318 source : AC1 19) chain A residue 245 type sequence A description BINDING SITE FOR RESIDUE NAP A 318 source : AC1 20) chain A residue 260 type sequence I description BINDING SITE FOR RESIDUE NAP A 318 source : AC1 21) chain A residue 261 type sequence P description BINDING SITE FOR RESIDUE NAP A 318 source : AC1 22) chain A residue 262 type sequence K description BINDING SITE FOR RESIDUE NAP A 318 source : AC1 23) chain A residue 263 type sequence S description BINDING SITE FOR RESIDUE NAP A 318 source : AC1 24) chain A residue 265 type sequence T description BINDING SITE FOR RESIDUE NAP A 318 source : AC1 25) chain A residue 268 type sequence R description BINDING SITE FOR RESIDUE NAP A 318 source : AC1 26) chain A residue 271 type sequence E description BINDING SITE FOR RESIDUE NAP A 318 source : AC1 27) chain A residue 272 type sequence N description BINDING SITE FOR RESIDUE NAP A 318 source : AC1 28) chain A residue 20 type sequence W description BINDING SITE FOR RESIDUE CIT A 319 source : AC2 29) chain A residue 48 type sequence Y description BINDING SITE FOR RESIDUE CIT A 319 source : AC2 30) chain A residue 79 type sequence W description BINDING SITE FOR RESIDUE CIT A 319 source : AC2 31) chain A residue 110 type sequence H description BINDING SITE FOR RESIDUE CIT A 319 source : AC2 32) chain A residue 111 type sequence W description BINDING SITE FOR RESIDUE CIT A 319 source : AC2 33) chain A residue 298 type sequence C description BINDING SITE FOR RESIDUE CIT A 319 source : AC2 34) chain A residue 20 type sequence W description BINDING SITE FOR RESIDUE FIS A 320 source : AC3 35) chain A residue 21 type sequence K description BINDING SITE FOR RESIDUE FIS A 320 source : AC3 36) chain A residue 218 type sequence P description BINDING SITE FOR RESIDUE FIS A 320 source : AC3 37) chain A residue 43 type catalytic sequence D description 725 source MCSA : MCSA1 38) chain A residue 48 type catalytic sequence Y description 725 source MCSA : MCSA1 39) chain A residue 77 type catalytic sequence K description 725 source MCSA : MCSA1 40) chain A residue 110 type catalytic sequence H description 725 source MCSA : MCSA1 41) chain A residue 48 type ACT_SITE sequence Y description Proton donor => ECO:0000269|PubMed:15272156 source Swiss-Prot : SWS_FT_FI1 42) chain A residue 9 type BINDING sequence G description BINDING => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 43) chain A residue 110 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3 44) chain A residue 210 type BINDING sequence S description BINDING => ECO:0000269|PubMed:15146478, ECO:0000269|PubMed:15272156, ECO:0000269|PubMed:16337231, ECO:0000269|PubMed:17368668, ECO:0000269|PubMed:17418233, ECO:0000269|PubMed:17505104 source Swiss-Prot : SWS_FT_FI4 45) chain A residue 77 type SITE sequence K description Lowers pKa of active site Tyr source Swiss-Prot : SWS_FT_FI5 46) chain A residue 1 type MOD_RES sequence A description N-acetylalanine => ECO:0000269|PubMed:8281941, ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI6 47) chain A residue 2 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P07943 source Swiss-Prot : SWS_FT_FI7 48) chain A residue 144-161 type prosite sequence MEELVDEGLVKAIGISNF description ALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. MeelvdeglVKAIGISNF source prosite : PS00062 49) chain A residue 260-275 type prosite sequence IPKSVTPERIAENFKV description ALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. IPKSVTpeRIaENfKV source prosite : PS00063 50) chain A residue 38-55 type prosite sequence GYRHIDCAHVYQNENEVG description ALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRHIDCAhvyqnEneVG source prosite : PS00798 51) chain A residue 94 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI8 52) chain A residue 221 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI8 53) chain A residue 262 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI8

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