eF-site ID 1bg9-A PDB Code 1bg9 Chain A click to enlarge Title BARLEY ALPHA-AMYLASE WITH SUBSTRATE ANALOGUE ACARBOSE Classification HYDROLASE Compound 1,4-ALPHA-D-GLUCAN GLUCANOHYDROLASE Source ORGANISM_SCIENTIFIC: Hordeum vulgare; Sequence A:  QVLFQGFNWESWKHNGGWYNFLMGKVDDIAAAGITHVWLP PASQSVAEQGYMPGRLYDLDASKYGNKAQLKSLIGALHGK GVKAIADIVINHRTAEHKDGRGIYCIFEGGTPDARLDWGP HMICRDDRPYADGTGNPDTGADFGAAPDIDHLNLRVQKEL VEWLNWLKADIGFDGWRFDFAKGYSADVAKIYIDRSEPSF AVAEIWTSLAYGGDGKPNLNQDQHRQELVNWVDKVGGKGP ATTFDFTTKGILNVAVEGELWRLRGTDGKAPGMIGWWPAK AVTFVDNHDTGSTQHMWPFPSDRVMQGYAYILTHPGTPCI FYDHFFDWGLKEEIDRLVSVRTRHGIHNESKLQIIEADAD LYLAEIDGKVIVKLGPRYDVGNLIPGGFKVAAHGNDYAVW EKI Description Functional site 1) chain A residue 179 type sequence D description source : AS 2) chain A residue 204 type sequence E description source : AS 3) chain A residue 289 type sequence D description source : AS 4) chain A residue 276 type sequence W description source : SS 5) chain A residue 277 type sequence W description source : SS 6) chain A residue 179 type ACT_SITE sequence D description Nucleophile => ECO:0000305|PubMed:9571044 source Swiss-Prot : SWS_FT_FI1 7) chain A residue 51 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:9571044 source Swiss-Prot : SWS_FT_FI3 8) chain A residue 177 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9571044 source Swiss-Prot : SWS_FT_FI3 9) chain A residue 206 type BINDING sequence W description BINDING => ECO:0000305|PubMed:9571044 source Swiss-Prot : SWS_FT_FI3 10) chain A residue 208 type BINDING sequence S description BINDING => ECO:0000305|PubMed:9571044 source Swiss-Prot : SWS_FT_FI3 11) chain A residue 226 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:9571044 source Swiss-Prot : SWS_FT_FI3 12) chain A residue 233 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9571044 source Swiss-Prot : SWS_FT_FI3 13) chain A residue 275 type BINDING sequence G description BINDING => ECO:0000305|PubMed:9571044 source Swiss-Prot : SWS_FT_FI3 14) chain A residue 288 type BINDING sequence H description BINDING => ECO:0000305|PubMed:9571044 source Swiss-Prot : SWS_FT_FI3 15) chain A residue 204 type ACT_SITE sequence E description Proton donor => ECO:0000305|PubMed:9571044 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 179 type catalytic sequence D description 397 source MCSA : MCSA1 17) chain A residue 204 type catalytic sequence E description 397 source MCSA : MCSA1 18) chain A residue 289 type catalytic sequence D description 397 source MCSA : MCSA1 19) chain A residue 269 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00693 source Swiss-Prot : SWS_FT_FI5 20) chain A residue 294 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P00693 source Swiss-Prot : SWS_FT_FI5 21) chain A residue 373 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00693 source Swiss-Prot : SWS_FT_FI5 22) chain A residue 390 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P00693 source Swiss-Prot : SWS_FT_FI5 23) chain A residue 400 type BINDING sequence W description BINDING => ECO:0000250|UniProtKB:P00693 source Swiss-Prot : SWS_FT_FI5 24) chain A residue 289 type SITE sequence D description Transition state stabilizer => ECO:0000305|PubMed:9571044 source Swiss-Prot : SWS_FT_FI6 25) chain A residue 91 type BINDING sequence N description BINDING => ECO:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702, ECO:0007744|PDB:1AVA source Swiss-Prot : SWS_FT_FI4 26) chain A residue 143 type BINDING sequence F description BINDING => ECO:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702, ECO:0007744|PDB:1AVA source Swiss-Prot : SWS_FT_FI4 27) chain A residue 146 type BINDING sequence A description BINDING => ECO:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702, ECO:0007744|PDB:1AVA source Swiss-Prot : SWS_FT_FI4 28) chain A residue 148 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702, ECO:0007744|PDB:1AVA source Swiss-Prot : SWS_FT_FI4 29) chain A residue 183 type BINDING sequence G description BINDING => ECO:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702, ECO:0007744|PDB:1AVA source Swiss-Prot : SWS_FT_FI4 30) chain A residue 108 type BINDING sequence E description BINDING => ECO:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702, ECO:0007744|PDB:1AVA source Swiss-Prot : SWS_FT_FI4 31) chain A residue 111 type BINDING sequence T description BINDING => ECO:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702, ECO:0007744|PDB:1AVA source Swiss-Prot : SWS_FT_FI4 32) chain A residue 113 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702, ECO:0007744|PDB:1AVA source Swiss-Prot : SWS_FT_FI4 33) chain A residue 117 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702, ECO:0007744|PDB:1AVA source Swiss-Prot : SWS_FT_FI4 34) chain A residue 127 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702, ECO:0007744|PDB:1AVA source Swiss-Prot : SWS_FT_FI4 35) chain A residue 138 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702, ECO:0007744|PDB:1AVA source Swiss-Prot : SWS_FT_FI4 36) chain A residue 141 type BINDING sequence A description BINDING => ECO:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702, ECO:0007744|PDB:1AVA source Swiss-Prot : SWS_FT_FI4 37) chain A residue 142 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8196040, ECO:0000269|PubMed:9571044, ECO:0000269|PubMed:9634702, ECO:0007744|PDB:1AVA source Swiss-Prot : SWS_FT_FI4

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