eF-site ID 1amy-A PDB Code 1amy Chain A click to enlarge Title CRYSTAL AND MOLECULAR STRUCTURE OF BARLEY ALPHA-AMYLASE Classification HYDROLASE (O-GLYCOSYL) Compound 1,4-ALPHA-D-GLUCAN GLUCANOHYDROLASE Source Hordeum vulgare (Barley) (AMY2_HORVU) 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 91 type sequence N description BINDING SITE FOR RESIDUE CA A 500 source : AC1 7) chain A residue 138 type sequence D description BINDING SITE FOR RESIDUE CA A 500 source : AC1 8) chain A residue 141 type sequence A description BINDING SITE FOR RESIDUE CA A 500 source : AC1 9) chain A residue 148 type sequence D description BINDING SITE FOR RESIDUE CA A 500 source : AC1 10) chain A residue 183 type sequence G description BINDING SITE FOR RESIDUE CA A 500 source : AC1 11) chain A residue 108 type sequence E description BINDING SITE FOR RESIDUE CA A 501 source : AC2 12) chain A residue 111 type sequence T description BINDING SITE FOR RESIDUE CA A 501 source : AC2 13) chain A residue 113 type sequence D description BINDING SITE FOR RESIDUE CA A 501 source : AC2 14) chain A residue 117 type sequence D description BINDING SITE FOR RESIDUE CA A 501 source : AC2 15) chain A residue 127 type sequence D description BINDING SITE FOR RESIDUE CA A 502 source : AC3 16) chain A residue 142 type sequence D description BINDING SITE FOR RESIDUE CA A 502 source : AC3 17) chain A residue 143 type sequence F description BINDING SITE FOR RESIDUE CA A 502 source : AC3 18) chain A residue 144 type sequence G description BINDING SITE FOR RESIDUE CA A 502 source : AC3 19) chain A residue 146 type sequence A description BINDING SITE FOR RESIDUE CA A 502 source : AC3 20) chain A residue 148 type sequence D description BINDING SITE FOR RESIDUE CA A 502 source : AC3 21) chain A residue 51 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:9571044 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 177 type BINDING sequence R description BINDING => ECO:0000305|PubMed:9571044 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 206 type BINDING sequence W description BINDING => ECO:0000305|PubMed:9571044 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 208 type BINDING sequence S description BINDING => ECO:0000305|PubMed:9571044 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 226 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:9571044 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 233 type BINDING sequence D description BINDING => ECO:0000305|PubMed:9571044 source Swiss-Prot : SWS_FT_FI3 27) chain A residue 275 type BINDING sequence G description BINDING => ECO:0000305|PubMed:9571044 source Swiss-Prot : SWS_FT_FI3 28) chain A residue 288 type BINDING sequence H description BINDING => ECO:0000305|PubMed:9571044 source Swiss-Prot : SWS_FT_FI3 29) 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 30) 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 31) 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 32) 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 33) 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 34) 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 35) 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 36) 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 37) 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 38) 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 39) 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 40) 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 41) 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 42) chain A residue 269 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00693 source Swiss-Prot : SWS_FT_FI5 43) chain A residue 294 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P00693 source Swiss-Prot : SWS_FT_FI5 44) chain A residue 373 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00693 source Swiss-Prot : SWS_FT_FI5 45) chain A residue 390 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P00693 source Swiss-Prot : SWS_FT_FI5 46) chain A residue 400 type BINDING sequence W description BINDING => ECO:0000250|UniProtKB:P00693 source Swiss-Prot : SWS_FT_FI5 47) chain A residue 289 type SITE sequence D description Transition state stabilizer => ECO:0000305|PubMed:9571044 source Swiss-Prot : SWS_FT_FI6 48) chain A residue 179 type ACT_SITE sequence D description Nucleophile => ECO:0000305|PubMed:9571044 source Swiss-Prot : SWS_FT_FI1 49) chain A residue 204 type ACT_SITE sequence E description Proton donor => ECO:0000305|PubMed:9571044 source Swiss-Prot : SWS_FT_FI2 50) chain A residue 179 type catalytic sequence D description 397 source MCSA : MCSA1 51) chain A residue 204 type catalytic sequence E description 397 source MCSA : MCSA1 52) chain A residue 289 type catalytic sequence D description 397 source MCSA : MCSA1

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