eF-site ID 1jda-A PDB Code 1jda Chain A click to enlarge Title MALTOTETRAOSE-FORMING EXO-AMYLASE Classification HYDROLASE Compound 1,4-ALPHA MALTOTETRAHYDROLASE Source Pseudomonas stutzeri (Pseudomonas perfectomarina) (AMT4_PSEST) Sequence A:  DQAGKSPNAVRYHGGDEIILQGFHWNVVREAPNDWYNILR QQAATIAADGFSAIWMPVPWRDFSSWSDGSKSGGGEGYFW HDFNKNGRYGSDAQLRQAASALGGAGVKVLYDVVPNHMNR GYPDKEINLPAGQGFWRNDCADPGNYPNDCDDGDRFIGGD ADLNTGHPQVYGMFRDEFTNLRSQYGAGGFRFDFVRGYAP ERVNSWMTDSADNSFCVGQLWKGPSEYPNWDWRNTASWQQ IIKDWSDRAKCPVFDFALKERMQNGSIADWKHGLNGNPDP RWREVAVTFVDNHDTGYSPGQNGGQHHWALQDGLIRQAYA YILTSPGTPVVYWDHMYDWGYGDFIRQLIQVRRAAGVRAD SAISFHSGYSGLVATVSGSQQTLVVALNSDLGNPGQVASG SFSEAVNASNGQVRVWRS Description Functional site 1) chain A residue 116 type sequence N description BINDING SITE FOR RESIDUE CA A 454 source : AC1 2) chain A residue 151 type sequence D description BINDING SITE FOR RESIDUE CA A 454 source : AC1 3) chain A residue 154 type sequence D description BINDING SITE FOR RESIDUE CA A 454 source : AC1 4) chain A residue 162 type sequence D description BINDING SITE FOR RESIDUE CA A 454 source : AC1 5) chain A residue 197 type sequence G description BINDING SITE FOR RESIDUE CA A 454 source : AC1 6) chain A residue 1 type sequence D description BINDING SITE FOR RESIDUE CA A 455 source : AC2 7) chain A residue 2 type sequence Q description BINDING SITE FOR RESIDUE CA A 455 source : AC2 8) chain A residue 13 type sequence H description BINDING SITE FOR RESIDUE CA A 455 source : AC2 9) chain A residue 16 type sequence D description BINDING SITE FOR RESIDUE CA A 455 source : AC2 10) chain A residue 17 type sequence E description BINDING SITE FOR RESIDUE CA A 455 source : AC2 11) chain A residue 193 type ACT_SITE sequence D description Nucleophile => ECO:0000305|PubMed:10556241 source Swiss-Prot : SWS_FT_FI1 12) chain A residue 219 type ACT_SITE sequence Q description Proton donor => ECO:0000305|PubMed:10556241, ECO:0000305|PubMed:9281429 source Swiss-Prot : SWS_FT_FI2 13) chain A residue 1 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10556241, ECO:0000269|PubMed:9126844, ECO:0000269|PubMed:9281429 source Swiss-Prot : SWS_FT_FI3 14) chain A residue 197 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10556241, ECO:0000269|PubMed:9126844, ECO:0000269|PubMed:9281429 source Swiss-Prot : SWS_FT_FI3 15) chain A residue 2 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:10556241, ECO:0000269|PubMed:9126844, ECO:0000269|PubMed:9281429 source Swiss-Prot : SWS_FT_FI3 16) chain A residue 13 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10556241, ECO:0000269|PubMed:9126844, ECO:0000269|PubMed:9281429 source Swiss-Prot : SWS_FT_FI3 17) chain A residue 16 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10556241, ECO:0000269|PubMed:9126844, ECO:0000269|PubMed:9281429 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 17 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10556241, ECO:0000269|PubMed:9126844, ECO:0000269|PubMed:9281429 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 116 type BINDING sequence N description BINDING => ECO:0000269|PubMed:10556241, ECO:0000269|PubMed:9126844, ECO:0000269|PubMed:9281429 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 151 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10556241, ECO:0000269|PubMed:9126844, ECO:0000269|PubMed:9281429 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 154 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10556241, ECO:0000269|PubMed:9126844, ECO:0000269|PubMed:9281429 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 162 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10556241, ECO:0000269|PubMed:9126844, ECO:0000269|PubMed:9281429 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 78 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:10556241 source Swiss-Prot : SWS_FT_FI4 24) chain A residue 156 type BINDING sequence F description BINDING => ECO:0000305|PubMed:10556241 source Swiss-Prot : SWS_FT_FI4 25) chain A residue 305 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:10556241 source Swiss-Prot : SWS_FT_FI4 26) chain A residue 117 type BINDING sequence H description BINDING => ECO:0000305|PubMed:10556241, ECO:0000305|PubMed:9281429 source Swiss-Prot : SWS_FT_FI5 27) chain A residue 191 type BINDING sequence R description BINDING => ECO:0000305|PubMed:10556241, ECO:0000305|PubMed:9281429 source Swiss-Prot : SWS_FT_FI5 28) chain A residue 293 type BINDING sequence H description BINDING => ECO:0000305|PubMed:10556241, ECO:0000305|PubMed:9281429 source Swiss-Prot : SWS_FT_FI5 29) chain A residue 196 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P0C1B3 source Swiss-Prot : SWS_FT_FI6 30) chain A residue 294 type SITE sequence D description Transition state stabilizer => ECO:0000305|PubMed:10556241 source Swiss-Prot : SWS_FT_FI7

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