eF-site ID 1qhp-A PDB Code 1qhp Chain A click to enlarge Title FIVE-DOMAIN ALPHA-AMYLASE FROM BACILLUS STEAROTHERMOPHILUS, MALTOSE COMPLEX Classification HYDROLASE Compound ALPHA-AMYLASE Source (AMYM_BACST) Sequence A:  SSSASVKGDVIYQIIIDRFYDGDTTNNNPAKSYGLYDPTK SKWKMYWGGDLEGVRQKLPYLKQLGVTTIWLSPVLDNLDT LAGTDNTGYHGYWTRDFKQIEEHFGNWTTFDTLVNDAHQN GIKVIVDFVPNHSTPFKANDSTFAEGGALYNNGTYMGNYF DDATKGYFHHNGDISNWDDRYEAQWKNFTDPAGFSLADLS QENGTIAQYLTDAAVQLVAHGADGLRIDAVKHFNSGFSKS LADKLYQKKDIFLVGEWYGDDPGTANHLEKVRYANNSGVN VLDFDLNTVIRNVFGTFTQTMYDLNNMVNQTGNEYKYKEN LITFIDNHDMSRFLSVNSNKANLHQALAFILTSRGTPSIY YGTEQYMAGGNDPYNRGMMPAFDTTTTAFKEVSTLAGLRR NNAAIQYGTTTQRWINNDVYIYERKFFNDVVLVAINRNTQ SSYSISGLQTALPNGSYADYLSGLLGGNGISVSNGSVASF TLAPGAVSVWQYSTSASAPQIGSVAPNMGIPGNVVTIDGK GFGTTQGTVTFGGVTATVKSWTSNRIEVYVPNMAAGLTDV KVTAGGVSSNLYSYNILSGTQTSVVFTVKSAPPTNLGDKI YLTGNIPELGNWSTDTSGAVNNAQGPLLAPNYPDWFYVFS VPAGKTIQFKFFIKRADGTIQWENGSNHVATTPTGATGNI TVTWQN Description Functional site 1) chain A residue 228 type catalytic sequence D description 905 source MCSA : MCSA1 2) chain A residue 256 type catalytic sequence E description 905 source MCSA : MCSA1 3) chain A residue 329 type catalytic sequence D description 905 source MCSA : MCSA1 4) chain A residue 256 type ACT_SITE sequence E description Proton donor => ECO:0000250|UniProtKB:P13507 source Swiss-Prot : SWS_FT_FI2 5) chain A residue 21 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO source Swiss-Prot : SWS_FT_FI3 6) chain A residue 101 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO source Swiss-Prot : SWS_FT_FI3 7) chain A residue 102 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO source Swiss-Prot : SWS_FT_FI3 8) chain A residue 131 type BINDING sequence N description BINDING => ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO source Swiss-Prot : SWS_FT_FI3 9) chain A residue 184 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO source Swiss-Prot : SWS_FT_FI3 10) chain A residue 198 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO source Swiss-Prot : SWS_FT_FI3 11) chain A residue 232 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO source Swiss-Prot : SWS_FT_FI3 12) chain A residue 23 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO source Swiss-Prot : SWS_FT_FI3 13) chain A residue 26 type BINDING sequence N description BINDING => ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO source Swiss-Prot : SWS_FT_FI3 14) chain A residue 27 type BINDING sequence N description BINDING => ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO source Swiss-Prot : SWS_FT_FI3 15) chain A residue 48 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO source Swiss-Prot : SWS_FT_FI3 16) chain A residue 50 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO source Swiss-Prot : SWS_FT_FI3 17) chain A residue 76 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO source Swiss-Prot : SWS_FT_FI3 18) chain A residue 77 type BINDING sequence N description BINDING => ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO source Swiss-Prot : SWS_FT_FI3 19) chain A residue 79 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10387084, ECO:0007744|PDB:1QHO source Swiss-Prot : SWS_FT_FI3 20) chain A residue 93 type BINDING sequence W description BINDING => ECO:0000250|UniProtKB:P0C1B3 source Swiss-Prot : SWS_FT_FI4 21) chain A residue 132 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P0C1B3 source Swiss-Prot : SWS_FT_FI4 22) chain A residue 226 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P0C1B3 source Swiss-Prot : SWS_FT_FI4 23) chain A residue 231 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P0C1B3 source Swiss-Prot : SWS_FT_FI4 24) chain A residue 259 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P0C1B3 source Swiss-Prot : SWS_FT_FI4 25) chain A residue 329 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P0C1B3 source Swiss-Prot : SWS_FT_FI4 26) chain A residue 376 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P0C1B3 source Swiss-Prot : SWS_FT_FI4 27) chain A residue 329 type SITE sequence D description Transition state stabilizer => ECO:0000250|UniProtKB:P0C1B3 source Swiss-Prot : SWS_FT_FI5 28) chain A residue 228 type ACT_SITE sequence D description Nucleophile => ECO:0000250|UniProtKB:P13507 source Swiss-Prot : SWS_FT_FI1

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