eF-site ID 1bya-A PDB Code 1bya Chain A click to enlarge Title CRYSTAL STRUCTURES OF SOYBEAN BETA-AMYLASE REACTED WITH BETA-MALTOSE AND MALTAL: ACTIVE SITE COMPONENTS AND THEIR APPARENT ROLE IN CATALYSIS Classification HYDROLASE(O-GLYCOSYL) Compound BETA-AMYLASE Source (AMYB_SOYBN) Sequence A:  SNMLLNYVPVYVMLPLGVVNVDNVFEDPDGLKEQLLQLRA AGVDGVMVDVWWGIIELKGPKQYDWRAYRSLFQLVQECGL TLQAIMSFHQCGGNVGDIVNIPIPQWVLDIGESNHDIFYT NRSGTRNKEYLTVGVDNEPIFHGRTAIEIYSDYMKSFREN MSDFLESGLIIDIEVGLGPAGELRYPSYPQSQGWEFPRIG EFQCYDKYLKADFKAAVARAGHPEWELPDDAGKYNDVPES TGFFKSNGTYVTEKGKFFLTWYSNKLLNHGDQILDEANKA FLGCKVKLAIKVSGIHWWYKVENHAAELTAGYYNLNDRDG YRPIARMLSRHHAILNFTCLEMRDSEQPSDAKSGPQELVQ QVLSGGWREDIRVAGENALPRYDATAYNQIILNAKPQGVN NNGPPKLSMFGVTYLRLSDDLLQKSNFNIFKKFVLKMHAD QDYCANPQKYNHAITPLKPSAPKIPIEVLLEATKPTLPFP WLPETDMKVDG Description Functional site 1) chain A residue 146 type sequence H description BINDING SITE FOR RESIDUE SO4 A 951 source : AC1 2) chain A residue 326 type sequence R description BINDING SITE FOR RESIDUE SO4 A 951 source : AC1 3) chain A residue 372 type sequence R description BINDING SITE FOR RESIDUE SO4 A 951 source : AC1 4) chain A residue 102 type catalytic sequence I description 436 source MCSA : MCSA1 5) chain A residue 187 type catalytic sequence L description 436 source MCSA : MCSA1 6) chain A residue 343 type catalytic sequence C description 436 source MCSA : MCSA1 7) chain A residue 381 type catalytic sequence N description 436 source MCSA : MCSA1 8) chain A residue 384 type catalytic sequence P description 436 source MCSA : MCSA1 9) chain A residue 187 type ACT_SITE sequence L description Proton donor => ECO:0000255|PROSITE-ProRule:PRU10050, ECO:0000269|PubMed:15178253, ECO:0000269|PubMed:2474529, ECO:0000269|PubMed:8011643, ECO:0000269|PubMed:8174545 source Swiss-Prot : SWS_FT_FI1 10) chain A residue 381 type ACT_SITE sequence N description Proton acceptor => ECO:0000269|PubMed:15178253, ECO:0000269|PubMed:8011643 source Swiss-Prot : SWS_FT_FI2 11) chain A residue 54 type BINDING sequence V description BINDING => ECO:0000269|PubMed:15178253 source Swiss-Prot : SWS_FT_FI3 12) chain A residue 94 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:15178253 source Swiss-Prot : SWS_FT_FI3 13) chain A residue 102 type BINDING sequence I description BINDING => ECO:0000269|PubMed:15178253 source Swiss-Prot : SWS_FT_FI3 14) chain A residue 296 type BINDING sequence V description BINDING => ECO:0000269|PubMed:15178253 source Swiss-Prot : SWS_FT_FI3 15) chain A residue 301 type BINDING sequence W description BINDING => ECO:0000269|PubMed:15178253 source Swiss-Prot : SWS_FT_FI3 16) chain A residue 343 type BINDING sequence C description BINDING => ECO:0000269|PubMed:15178253 source Swiss-Prot : SWS_FT_FI3 17) chain A residue 382 type BINDING sequence A description BINDING => ECO:0000269|PubMed:15178253 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 421 type BINDING sequence L description BINDING => ECO:0000269|PubMed:15178253 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 93-101 type prosite sequence HQCGGNVGD description BETA_AMYLASE_1 Beta-amylase active site 1. HqCGGNVGD source prosite : PS00506 20) chain A residue 182-192 type prosite sequence GPAGELRYPSY description BETA_AMYLASE_2 Beta-amylase active site 2. GpAGELRYPSY source prosite : PS00679

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