eF-site ID 1bpl-AB PDB Code 1bpl Chain A, B click to enlarge Title GLYCOSYLTRANSFERASE Classification GLYCOSYLTRANSFERASE Compound ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE Source ORGANISM_SCIENTIFIC: Bacillus licheniformis; Sequence A:  LNGTLMQYFEWYMPNDGQHWKRLQNDSAYLAEHGITAVWI PPAYKGTSQADVGYGAYDLYDLGEFHQKGTVRTKYGTKGE LQSAIKSLHSRDINVYGDVVINHKGGADATEDVTAVEVDP ADRNRVISGEHLIKAWTHFHFPGRGSTYSDFKWHWYHFDG TDWDESRKLNRIYKFQGKA B:  YDYLMYADIDYDHPDVAAEIKRWGTWYANELQLDGFRLDA VKHIKFSFLRDWVNHVREKTGKEMFTVAEYWQNDLGALEN YLNKTNFNHSVFDVPLHYQFHAASTQGGGYDMRKLLNSTV VSKHPLKAVTFVDNHDTQPGQSLESTVQTWFKPLAYAFIL TRESGYPQVFYGDMYGTKGDSQREIPALKHKIEPILKARK QYAYGAQHDYFDHHDIVGWTREGDSSVANSGLAALITDGP GGAKRMYVGRQNAGETWHDITGNRSEPVVINSEGWGEFHV NGGSVSIYVQ Description Functional site 1) chain B residue 231 type sequence D description ACTIVE SITE CATALYTIC RESIDUES source : ACT 2) chain B residue 261 type sequence E description ACTIVE SITE CATALYTIC RESIDUES source : ACT 3) chain B residue 328 type sequence D description ACTIVE SITE CATALYTIC RESIDUES source : ACT 4) chain B residue 328 type SITE sequence D description Transition state stabilizer => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 5) chain B residue 194 type BINDING sequence D description BINDING => ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551 source Swiss-Prot : SWS_FT_FI3 6) chain B residue 200 type BINDING sequence D description BINDING => ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551 source Swiss-Prot : SWS_FT_FI3 7) chain B residue 204 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_FI4 8) chain B residue 300 type BINDING sequence G description BINDING => ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0 source Swiss-Prot : SWS_FT_FI4 9) chain B 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_FI4 10) chain B 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_FI4 11) chain B 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_FI4 12) chain B 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_FI4 13) chain B residue 202 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_FI4 14) chain B residue 235 type BINDING sequence H description BINDING => ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0 source Swiss-Prot : SWS_FT_FI5 15) chain A residue 181 type ACT_SITE sequence A description Nucleophile source Swiss-Prot : SWS_FT_FI1 16) chain B residue 231 type ACT_SITE sequence D description Nucleophile source Swiss-Prot : SWS_FT_FI1 17) chain B residue 261 type ACT_SITE sequence E description Proton donor source Swiss-Prot : SWS_FT_FI2

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