eF-site ID 2alr-A PDB Code 2alr Chain A click to enlarge Title ALDEHYDE REDUCTASE Classification OXIDOREDUCTASE Compound ALDEHYDE REDUCTASE Source ORGANISM_COMMON: human; ORGANISM_SCIENTIFIC: Homo sapiens; Sequence A:  AASCVLLHTGQKMPLIGLGTWKSEPGQVKAAVKYALSVGY RHIDCAAIYGNEPEIGEALKEDVGPGKAVPREELFVTSKL WNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAFERG DNPFPKNADGTICYDSTHYKETWKALEALVAKGLVQALGL SNFNSRQIDDILSVASVRPAVLQVECHPYLAQNELIAHCQ ARGLEVTAYSPLGVLLEEPVVLALAEKYGRSPAQILLRWQ VQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALN KNWRYIVPMLTVDGKRVPRDAGHPLYPFNDPY Description Functional site 1) chain A residue 146-163 type prosite sequence LEALVAKGLVQALGLSNF description ALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. LealvakglVQALGLSNF source prosite : PS00062 2) chain A residue 260-275 type prosite sequence IPKSITPSRILQNIKV description ALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. IPKSITpsRIlQNiKV source prosite : PS00063 3) chain A residue 39-56 type prosite sequence GYRHIDCAAIYGNEPEIG description ALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRHIDCAaiygnEpeIG source prosite : PS00798 4) chain A residue 50 type ACT_SITE sequence G description Proton donor => ECO:0000269|PubMed:7669785, ECO:0000305|PubMed:30538128, ECO:0000305|PubMed:31649033 source Swiss-Prot : SWS_FT_FI1 5) chain A residue 211 type MOD_RES sequence P description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI10 6) chain A residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:O60218 source Swiss-Prot : SWS_FT_FI2 7) chain A residue 21 type BINDING sequence W description BINDING => ECO:0000250|UniProtKB:P50578 source Swiss-Prot : SWS_FT_FI3 8) chain A residue 263 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P50578 source Swiss-Prot : SWS_FT_FI3 9) chain A residue 264 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:P50578 source Swiss-Prot : SWS_FT_FI3 10) chain A residue 265 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P50578 source Swiss-Prot : SWS_FT_FI3 11) chain A residue 266 type BINDING sequence P description BINDING => ECO:0000250|UniProtKB:P50578 source Swiss-Prot : SWS_FT_FI3 12) chain A residue 269 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:P50578 source Swiss-Prot : SWS_FT_FI3 13) chain A residue 272 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P50578 source Swiss-Prot : SWS_FT_FI3 14) chain A residue 273 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:P50578 source Swiss-Prot : SWS_FT_FI3 15) chain A residue 22 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P50578 source Swiss-Prot : SWS_FT_FI3 16) chain A residue 45 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:P50578 source Swiss-Prot : SWS_FT_FI3 17) chain A residue 162 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P50578 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 163 type BINDING sequence F description BINDING => ECO:0000250|UniProtKB:P50578 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 211 type BINDING sequence P description BINDING => ECO:0000250|UniProtKB:P50578 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 213 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P50578 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 80 type SITE sequence L description Lowers pKa of active site Tyr => ECO:0000269|PubMed:7669785 source Swiss-Prot : SWS_FT_FI4 22) chain A residue 2 type MOD_RES sequence A description N-acetylalanine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI5 23) chain A residue 4 type MOD_RES sequence C description Phosphoserine => ECO:0000250|UniProtKB:P51635 source Swiss-Prot : SWS_FT_FI6 24) chain A residue 38 type MOD_RES sequence V description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 25) chain A residue 127 type MOD_RES sequence N description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9JII6 source Swiss-Prot : SWS_FT_FI8 26) chain A residue 145 type MOD_RES sequence A description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JII6 source Swiss-Prot : SWS_FT_FI9

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