eF-site ID 1hqt-A PDB Code 1hqt Chain A click to enlarge Title THE CRYSTAL STRUCTURE OF AN ALDEHYDE REDUCTASE Y50F MUTANT-NADP COMPLEX AND ITS IMPLICATIONS FOR SUBSTRATE BINDING Classification OXIDOREDUCTASE Compound ALDEHYDE REDUCTASE Source null (AK1A1_PIG) Sequence A:  AASCVLLHTGQKMPLIGLGTWKSEPGQVKAAIKYALTVGY RHIDCAAIFGNELEIGEALQETVGPGKAVPREELFVTSKL WNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAFERG DNPFPKNADGTIRYDATHYKDTWKALEALVAKGLVRALGL SNFSSRQIDDVLSVASVRPAVLQVECHPYLAQNELIAHCQ ARGLEVTAYSPLGSSDRAWRDPNEPVLLEEPVVQALAEKY NRSPAQILLRWQVQRKVICIPKSVTPSRIPQNIQVFDFTF SPEEMKQLDALNKNLRFIVPMLTVDGKRVPRDAGHPLYPF NDPY Description Functional site 1) chain A residue 20 type sequence G description BINDING SITE FOR RESIDUE NAP A 350 source : AC1 2) chain A residue 21 type sequence T description BINDING SITE FOR RESIDUE NAP A 350 source : AC1 3) chain A residue 22 type sequence W description BINDING SITE FOR RESIDUE NAP A 350 source : AC1 4) chain A residue 45 type sequence D description BINDING SITE FOR RESIDUE NAP A 350 source : AC1 5) chain A residue 80 type sequence K description BINDING SITE FOR RESIDUE NAP A 350 source : AC1 6) chain A residue 113 type sequence H description BINDING SITE FOR RESIDUE NAP A 350 source : AC1 7) chain A residue 162 type sequence S description BINDING SITE FOR RESIDUE NAP A 350 source : AC1 8) chain A residue 163 type sequence N description BINDING SITE FOR RESIDUE NAP A 350 source : AC1 9) chain A residue 184 type sequence Q description BINDING SITE FOR RESIDUE NAP A 350 source : AC1 10) chain A residue 210 type sequence Y description BINDING SITE FOR RESIDUE NAP A 350 source : AC1 11) chain A residue 211 type sequence S description BINDING SITE FOR RESIDUE NAP A 350 source : AC1 12) chain A residue 212 type sequence P description BINDING SITE FOR RESIDUE NAP A 350 source : AC1 13) chain A residue 213 type sequence L description BINDING SITE FOR RESIDUE NAP A 350 source : AC1 14) chain A residue 214 type sequence G description BINDING SITE FOR RESIDUE NAP A 350 source : AC1 15) chain A residue 215 type sequence S description BINDING SITE FOR RESIDUE NAP A 350 source : AC1 16) chain A residue 216 type sequence S description BINDING SITE FOR RESIDUE NAP A 350 source : AC1 17) chain A residue 246 type sequence A description BINDING SITE FOR RESIDUE NAP A 350 source : AC1 18) chain A residue 261 type sequence I description BINDING SITE FOR RESIDUE NAP A 350 source : AC1 19) chain A residue 262 type sequence P description BINDING SITE FOR RESIDUE NAP A 350 source : AC1 20) chain A residue 263 type sequence K description BINDING SITE FOR RESIDUE NAP A 350 source : AC1 21) chain A residue 264 type sequence S description BINDING SITE FOR RESIDUE NAP A 350 source : AC1 22) chain A residue 265 type sequence V description BINDING SITE FOR RESIDUE NAP A 350 source : AC1 23) chain A residue 266 type sequence T description BINDING SITE FOR RESIDUE NAP A 350 source : AC1 24) chain A residue 269 type sequence R description BINDING SITE FOR RESIDUE NAP A 350 source : AC1 25) chain A residue 273 type sequence N description BINDING SITE FOR RESIDUE NAP A 350 source : AC1 26) chain A residue 211 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P14550 source Swiss-Prot : SWS_FT_FI10 27) chain A residue 50 type ACT_SITE sequence F description Proton donor => ECO:0000269|PubMed:7552731 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 147-164 type prosite sequence LEALVAKGLVRALGLSNF description ALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. LealvakglVRALGLSNF source prosite : PS00062 29) chain A residue 261-276 type prosite sequence IPKSVTPSRIPQNIQV description ALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. IPKSVTpsRIpQNiQV source prosite : PS00063 30) chain A residue 40-57 type prosite sequence GYRHIDCAAIFGNELEIG description ALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRHIDCAaifgnEleIG source prosite : PS00798 31) chain A residue 11 type BINDING sequence G description BINDING => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 32) chain A residue 21 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:O60218 source Swiss-Prot : SWS_FT_FI3 33) chain A residue 45 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:O60218 source Swiss-Prot : SWS_FT_FI3 34) chain A residue 162 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:O60218 source Swiss-Prot : SWS_FT_FI3 35) chain A residue 184 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:O60218 source Swiss-Prot : SWS_FT_FI3 36) chain A residue 113 type BINDING sequence H description BINDING => ECO:0000269|PubMed:7552731 source Swiss-Prot : SWS_FT_FI4 37) chain A residue 211 type BINDING sequence S description BINDING => ECO:0000269|PubMed:7552731 source Swiss-Prot : SWS_FT_FI4 38) chain A residue 80 type SITE sequence K description Lowers pKa of active site Tyr => ECO:0000250|UniProtKB:P14550 source Swiss-Prot : SWS_FT_FI5 39) chain A residue 2 type MOD_RES sequence A description N-acetylalanine => ECO:0000250|UniProtKB:P14550 source Swiss-Prot : SWS_FT_FI6 40) chain A residue 4 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P51635 source Swiss-Prot : SWS_FT_FI7 41) chain A residue 127 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9JII6 source Swiss-Prot : SWS_FT_FI8 42) chain A residue 145 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JII6 source Swiss-Prot : SWS_FT_FI9

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