eF-site ID 1e3x-A PDB Code 1e3x Chain A click to enlarge Title Native structure of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.92A Classification HYDROLASE Compound ALPHA-AMYLASE Source (AMY_BACLI) Sequence A:  VNGTLMQYFEWYTPNDGQHWKRLQNDAEHLSDIGITAVWI PPAYKGLSQSDNGYGPYDLYDLGEFQQKGTVRTKYGTKSE LQDAIGSLHSRNVQVYGDVVLNHKAGADATEDVTAVEVNP ANRNQETSEEYQIKAWTDFRFPGRGNTYSDFKWHWYHFDG ADWDESRKISRIFKFRGEGKAWDWEVSSENGNYDYLMYAD VDYDHPDVVAETKKWGIWYANELSLDGFRIDAAKHIKFSF LRDWVQAVRQATGKEMFTVAEYWQNNAGKLENYLNKTSFN QSVFDVPLHFNLQAASSQGGGYDMRKLLNGTVVSKHPLKS VTFVDNHDTQPGQSLESTVQTWFKPLAYAFILTRESGYPQ VFYGDMYGTKGDSQREIPALKHKIEPILKARKQYAYGAQH DYFDHHDIVGWTREGDSSVANSGLAALITDGPGGAKRMYV GRQNAGETWHDITGNRSEPVVINSEGWGEFHVNGGSVSIY VQR Description (1)  ALPHA-AMYLASE (E.C.3.2.1.1) Functional site 1) chain A residue 102 type sequence N description BINDING SITE FOR RESIDUE CA A 501 source : AC1 2) chain A residue 194 type sequence D description BINDING SITE FOR RESIDUE CA A 501 source : AC1 3) chain A residue 200 type sequence D description BINDING SITE FOR RESIDUE CA A 501 source : AC1 4) chain A residue 235 type sequence H description BINDING SITE FOR RESIDUE CA A 501 source : AC1 5) chain A residue 159 type sequence D description BINDING SITE FOR RESIDUE CA A 502 source : AC2 6) chain A residue 181 type sequence A description BINDING SITE FOR RESIDUE CA A 502 source : AC2 7) chain A residue 183 type sequence D description BINDING SITE FOR RESIDUE CA A 502 source : AC2 8) chain A residue 202 type sequence D description BINDING SITE FOR RESIDUE CA A 502 source : AC2 9) chain A residue 204 type sequence D description BINDING SITE FOR RESIDUE CA A 502 source : AC2 10) chain A residue 444 type sequence N description BINDING SITE FOR RESIDUE CA A 503 source : AC3 11) chain A residue 447 type sequence E description BINDING SITE FOR RESIDUE CA A 503 source : AC3 12) chain A residue 300 type sequence G description BINDING SITE FOR RESIDUE CA A 504 source : AC4 13) chain A residue 302 type sequence Y description BINDING SITE FOR RESIDUE CA A 504 source : AC4 14) chain A residue 406 type sequence H description BINDING SITE FOR RESIDUE CA A 504 source : AC4 15) chain A residue 407 type sequence D description BINDING SITE FOR RESIDUE CA A 504 source : AC4 16) chain A residue 430 type sequence D description BINDING SITE FOR RESIDUE CA A 504 source : AC4 17) chain A residue 159 type sequence D description BINDING SITE FOR RESIDUE NA A 505 source : AC5 18) chain A residue 183 type sequence D description BINDING SITE FOR RESIDUE NA A 505 source : AC5 19) chain A residue 194 type sequence D description BINDING SITE FOR RESIDUE NA A 505 source : AC5 20) chain A residue 200 type sequence D description BINDING SITE FOR RESIDUE NA A 505 source : AC5 21) chain A residue 201 type sequence V description BINDING SITE FOR RESIDUE NA A 505 source : AC5 22) chain A residue 102 type BINDING sequence N description BINDING => ECO:0000269|PubMed:10924103, ECO:0000269|PubMed:20124706, ECO:0007744|PDB:1E40 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 181 type BINDING sequence A description BINDING => ECO:0000269|PubMed:10924103, ECO:0000269|PubMed:20124706, ECO:0007744|PDB:1E40 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 202 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10924103, ECO:0000269|PubMed:20124706, ECO:0007744|PDB:1E40 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 204 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10924103, ECO:0000269|PubMed:20124706, ECO:0007744|PDB:1E40 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 235 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10924103, ECO:0000269|PubMed:20124706, ECO:0007744|PDB:1E40 source Swiss-Prot : SWS_FT_FI3 27) chain A residue 159 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10924103, ECO:0007744|PDB:1E40 source Swiss-Prot : SWS_FT_FI4 28) chain A residue 183 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10924103, ECO:0007744|PDB:1E40 source Swiss-Prot : SWS_FT_FI4 29) chain A residue 194 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10924103, ECO:0007744|PDB:1E40 source Swiss-Prot : SWS_FT_FI4 30) chain A residue 200 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10924103, ECO:0007744|PDB:1E40 source Swiss-Prot : SWS_FT_FI4 31) chain A residue 300 type BINDING sequence G description BINDING => ECO:0000269|PubMed:20124706, ECO:0007744|PDB:3BH4 source Swiss-Prot : SWS_FT_FI5 32) chain A residue 407 type BINDING sequence D description BINDING => ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0 source Swiss-Prot : SWS_FT_FI6 33) chain A residue 430 type BINDING sequence D description BINDING => ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0 source Swiss-Prot : SWS_FT_FI6 34) chain A residue 302 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0 source Swiss-Prot : SWS_FT_FI6 35) chain A residue 406 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0 source Swiss-Prot : SWS_FT_FI6 36) chain A residue 231 type ACT_SITE sequence D description Nucleophile source Swiss-Prot : SWS_FT_FI1 37) chain A residue 261 type ACT_SITE sequence E description Proton donor source Swiss-Prot : SWS_FT_FI2 38) chain A residue 328 type SITE sequence D description Transition state stabilizer => ECO:0000250 source Swiss-Prot : SWS_FT_FI7

Display surface Download Links