eF-site ID 1l0p-A PDB Code 1l0p Chain A click to enlarge Title CRYSTAL STRUCTURE ANALYSIS OF THE COMPLEX BETWEEN PSYCHROPHILIC ALPHA AMYLASE FROM PSEUDOALTEROMONAS HALOPLANCTIS AND NITRATE Classification HYDROLASE Compound ALPHA-AMYLASE Source ORGANISM_SCIENTIFIC: Pseudoalteromonas haloplanktis; Sequence A:  TPTTFVHLFEWNWQDVAQECEQYLGPKGYAAVQVSPPNEH ITGSQWWTRYQPVSYELQSRGGNRAQFIDMVNRCSAAGVD IYVDTLINHMAAGSGTGTAGNSFGNKSFPIYSPQDFHESC TINNSDYGNDRYRVQNCELVGLADLDTASNYVQNTIAAYI NDLQAIGVKGFRFDASKHVAASDIQSLMAKVNGSPVVFQE VIDQGGEAVGASEYLSTGLVTEFKYSTELGNTFRNGSLAW LSNFGEGWGFMPSSSAVVFVDNHDNQRGHGGAGNVITFED GRLYDLANVFMLAYPYGYPKVMSSYDFHGDTDAGGPNVPV HNNGNLECFASNWKCEHRWSYIAGGVDFRNNTADNWAVTN WWDNTNNQISFGRGSSGHMAINKEDSTLTATVQTDMASGQ YCNVLKGELSADAKSCSGEVITVNSDGTINLNIGAWDAMA IHKNAKLN Description Functional site 1) chain A residue 88 type sequence N description BINDING SITE FOR RESIDUE CA A 800 source : AC1 2) chain A residue 135 type sequence Q description BINDING SITE FOR RESIDUE CA A 800 source : AC1 3) chain A residue 144 type sequence D description BINDING SITE FOR RESIDUE CA A 800 source : AC1 4) chain A residue 178 type sequence H description BINDING SITE FOR RESIDUE CA A 800 source : AC1 5) chain A residue 172 type sequence R description BINDING SITE FOR RESIDUE NO3 A 901 source : AC2 6) chain A residue 200 type sequence E description BINDING SITE FOR RESIDUE NO3 A 901 source : AC2 7) chain A residue 221 type sequence T description BINDING SITE FOR RESIDUE NO3 A 901 source : AC2 8) chain A residue 259 type sequence F description BINDING SITE FOR RESIDUE NO3 A 901 source : AC2 9) chain A residue 262 type sequence N description BINDING SITE FOR RESIDUE NO3 A 901 source : AC2 10) chain A residue 300 type sequence K description BINDING SITE FOR RESIDUE NO3 A 901 source : AC2 11) chain A residue 300 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11914073, ECO:0000269|PubMed:9541387, ECO:0007744|PDB:1AQH source Swiss-Prot : SWS_FT_FI7 12) chain A residue 47 type BINDING sequence W description BINDING => ECO:0000305|PubMed:11914073 source Swiss-Prot : SWS_FT_FI3 13) chain A residue 89 type BINDING sequence H description BINDING => ECO:0000305|PubMed:11914073 source Swiss-Prot : SWS_FT_FI3 14) chain A residue 177 type BINDING sequence K description BINDING => ECO:0000305|PubMed:11914073 source Swiss-Prot : SWS_FT_FI3 15) chain A residue 207 type BINDING sequence E description BINDING => ECO:0000305|PubMed:11914073 source Swiss-Prot : SWS_FT_FI3 16) chain A residue 264 type BINDING sequence D description BINDING => ECO:0000305|PubMed:11914073 source Swiss-Prot : SWS_FT_FI3 17) chain A residue 269 type BINDING sequence H description BINDING => ECO:0000305|PubMed:11914073 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 88 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11914073, ECO:0000269|PubMed:12021442, ECO:0000269|PubMed:9541387, ECO:0007744|PDB:1AQH source Swiss-Prot : SWS_FT_FI4 19) chain A residue 135 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:11914073, ECO:0000269|PubMed:12021442, ECO:0000269|PubMed:9541387, ECO:0007744|PDB:1AQH source Swiss-Prot : SWS_FT_FI4 20) chain A residue 144 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11914073, ECO:0000269|PubMed:12021442, ECO:0000269|PubMed:9541387, ECO:0007744|PDB:1AQH source Swiss-Prot : SWS_FT_FI4 21) chain A residue 178 type BINDING sequence H description BINDING => ECO:0000269|PubMed:11914073, ECO:0000269|PubMed:12021442, ECO:0000269|PubMed:9541387, ECO:0007744|PDB:1AQH source Swiss-Prot : SWS_FT_FI4 22) chain A residue 172 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 23) chain A residue 262 type BINDING sequence N description BINDING => ECO:0000269|PubMed:9541387, ECO:0007744|PDB:1AQH source Swiss-Prot : SWS_FT_FI6 24) chain A residue 174 type ACT_SITE sequence D description Nucleophile => ECO:0000269|PubMed:11914073 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 200 type ACT_SITE sequence E description Proton donor => ECO:0000269|PubMed:11914073 source Swiss-Prot : SWS_FT_FI2 26) chain A residue 264 type SITE sequence D description Transition state stabilizer => ECO:0000250 source Swiss-Prot : SWS_FT_FI8

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