eF-site ID 2ceq-AB PDB Code 2ceq Chain A, B click to enlarge Title Beta-glycosidase from Sulfolobus solfataricus in complex with glucoimidazole Classification HYDROLASE Compound BETA-GALACTOSIDASE Source null (BGAL_SULSO) Sequence A:  MYSFPNSFRFGWSQAGFQSEMGTPGSEDPNTDWYKWVHDP ENMAAGLVSGDLPENGPGYWGNYKTFHDNAQKMGLKIARL NVEWSRIFPNPLPRPQNFDESKQDVTEVEINENELKRLDE YANKDALNHYREIFKDLKSRGLYFILNMYHWPLPLWLHDP IRVRRGDFTGPSGWLSTRTVYEFARFSAYIAWKFDDLVDE YSTMNEPNVVGGLGYVGVKSGFPPGYLSFELSRRAMYNII QAHARAYDGIKSVSKKPVGIIYANSSFQPLTDKDMEAVEM AENDNRWWFFDAIIRGEITRGNEKIVRDDLKGRLDWIGVN YYTRTVVKRTEKGYVSLGGYGHGCERNSVSLAGLPTSDFG WEFFPEGLYDVLTKYWNRYHLYMYVTENGIADDADYQRPY YLVSHVYQVHRAINSGADVRGYLHWSLADNYEWASGFSMR FGLLKVDYNTKRLYWRPSALVYREIATNGAITDEIEHLNS VPPVKPLRH B:  MYSFPNSFRFGWSQAGFQSEMGTPGSEDPNTDWYKWVHDP ENMAAGLVSGDLPENGPGYWGNYKTFHDNAQKMGLKIARL NVEWSRIFPNPLPRPQNFDESKQDVTEVEINENELKRLDE YANKDALNHYREIFKDLKSRGLYFILNMYHWPLPLWLHDP IRVRRGDFTGPSGWLSTRTVYEFARFSAYIAWKFDDLVDE YSTMNEPNVVGGLGYVGVKSGFPPGYLSFELSRRAMYNII QAHARAYDGIKSVSKKPVGIIYANSSFQPLTDKDMEAVEM AENDNRWWFFDAIIRGEITRGNEKIVRDDLKGRLDWIGVN YYTRTVVKRTEKGYVSLGGYGHGCERNSVSLAGLPTSDFG WEFFPEGLYDVLTKYWNRYHLYMYVTENGIADDADYQRPY YLVSHVYQVHRAINSGADVRGYLHWSLADNYEWASGFSMR FGLLKVDYNTKRLYWRPSALVYREIATNGAITDEIEHLNS VPPVKPLRH Description Functional site 1) chain A residue 46 type sequence G description BINDING SITE FOR RESIDUE ACT A1490 source : AC1 2) chain A residue 49 type sequence S description BINDING SITE FOR RESIDUE ACT A1490 source : AC1 3) chain A residue 434 type sequence A description BINDING SITE FOR RESIDUE ACT A1490 source : AC1 4) chain A residue 234 type sequence R description BINDING SITE FOR RESIDUE ACT A1491 source : AC2 5) chain A residue 113 type sequence N description BINDING SITE FOR RESIDUE ACT B1490 source : AC3 6) chain B residue 2 type sequence Y description BINDING SITE FOR RESIDUE ACT B1490 source : AC3 7) chain B residue 410 type sequence H description BINDING SITE FOR RESIDUE ACT B1490 source : AC3 8) chain B residue 414 type sequence N description BINDING SITE FOR RESIDUE ACT B1490 source : AC3 9) chain B residue 323 type sequence T description BINDING SITE FOR RESIDUE ACT B1491 source : AC4 10) chain B residue 342 type sequence H description BINDING SITE FOR RESIDUE ACT B1491 source : AC4 11) chain B residue 455 type sequence W description BINDING SITE FOR RESIDUE ACT B1492 source : AC5 12) chain B residue 463 type sequence R description BINDING SITE FOR RESIDUE ACT B1492 source : AC5 13) chain B residue 464 type sequence E description BINDING SITE FOR RESIDUE ACT B1492 source : AC5 14) chain B residue 474 type sequence E description BINDING SITE FOR RESIDUE ACT B1492 source : AC5 15) chain A residue 18 type sequence Q description BINDING SITE FOR RESIDUE GIM A1492 source : AC6 16) chain A residue 150 type sequence H description BINDING SITE FOR RESIDUE GIM A1492 source : AC6 17) chain A residue 151 type sequence W description BINDING SITE FOR RESIDUE GIM A1492 source : AC6 18) chain A residue 205 type sequence N description BINDING SITE FOR RESIDUE GIM A1492 source : AC6 19) chain A residue 206 type sequence E description BINDING SITE FOR RESIDUE GIM A1492 source : AC6 20) chain A residue 322 type sequence Y description BINDING SITE FOR RESIDUE GIM A1492 source : AC6 21) chain A residue 361 type sequence W description BINDING SITE FOR RESIDUE GIM A1492 source : AC6 22) chain A residue 387 type sequence E description BINDING SITE FOR RESIDUE GIM A1492 source : AC6 23) chain A residue 425 type sequence W description BINDING SITE FOR RESIDUE GIM A1492 source : AC6 24) chain A residue 432 type sequence E description BINDING SITE FOR RESIDUE GIM A1492 source : AC6 25) chain A residue 433 type sequence W description BINDING SITE FOR RESIDUE GIM A1492 source : AC6 26) chain A residue 441 type sequence F description BINDING SITE FOR RESIDUE GIM A1492 source : AC6 27) chain B residue 18 type sequence Q description BINDING SITE FOR RESIDUE GIM B1493 source : AC7 28) chain B residue 150 type sequence H description BINDING SITE FOR RESIDUE GIM B1493 source : AC7 29) chain B residue 205 type sequence N description BINDING SITE FOR RESIDUE GIM B1493 source : AC7 30) chain B residue 206 type sequence E description BINDING SITE FOR RESIDUE GIM B1493 source : AC7 31) chain B residue 322 type sequence Y description BINDING SITE FOR RESIDUE GIM B1493 source : AC7 32) chain B residue 361 type sequence W description BINDING SITE FOR RESIDUE GIM B1493 source : AC7 33) chain B residue 387 type sequence E description BINDING SITE FOR RESIDUE GIM B1493 source : AC7 34) chain B residue 425 type sequence W description BINDING SITE FOR RESIDUE GIM B1493 source : AC7 35) chain B residue 432 type sequence E description BINDING SITE FOR RESIDUE GIM B1493 source : AC7 36) chain B residue 433 type sequence W description BINDING SITE FOR RESIDUE GIM B1493 source : AC7 37) chain B residue 441 type sequence F description BINDING SITE FOR RESIDUE GIM B1493 source : AC7 38) chain B residue 206 type ACT_SITE sequence E description Proton donor => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 39) chain A residue 206 type ACT_SITE sequence E description Proton donor => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 40) chain B residue 387 type ACT_SITE sequence E description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10055 source Swiss-Prot : SWS_FT_FI2 41) chain A residue 387 type ACT_SITE sequence E description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10055 source Swiss-Prot : SWS_FT_FI2 42) chain A residue 273 type MOD_RES sequence K description N6-methyllysine; partial => ECO:0000269|PubMed:14660666 source Swiss-Prot : SWS_FT_FI4 43) chain A residue 311 type MOD_RES sequence K description N6-methyllysine; partial => ECO:0000269|PubMed:14660666 source Swiss-Prot : SWS_FT_FI4 44) chain B residue 116 type MOD_RES sequence K description N6-methyllysine; partial => ECO:0000269|PubMed:14660666 source Swiss-Prot : SWS_FT_FI4 45) chain B residue 273 type MOD_RES sequence K description N6-methyllysine; partial => ECO:0000269|PubMed:14660666 source Swiss-Prot : SWS_FT_FI4 46) chain B residue 311 type MOD_RES sequence K description N6-methyllysine; partial => ECO:0000269|PubMed:14660666 source Swiss-Prot : SWS_FT_FI4 47) chain A residue 116 type MOD_RES sequence K description N6-methyllysine; partial => ECO:0000269|PubMed:14660666 source Swiss-Prot : SWS_FT_FI4 48) chain A residue 332 type MOD_RES sequence K description N6-methyllysine => ECO:0000269|PubMed:14660666 source Swiss-Prot : SWS_FT_FI5 49) chain B residue 135 type MOD_RES sequence K description N6-methyllysine => ECO:0000269|PubMed:14660666 source Swiss-Prot : SWS_FT_FI5 50) chain B residue 332 type MOD_RES sequence K description N6-methyllysine => ECO:0000269|PubMed:14660666 source Swiss-Prot : SWS_FT_FI5 51) chain A residue 135 type MOD_RES sequence K description N6-methyllysine => ECO:0000269|PubMed:14660666 source Swiss-Prot : SWS_FT_FI5 52) chain A residue 383-391 type prosite sequence MYVTENGIA description GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. MYVTENGIA source prosite : PS00572 53) chain A residue 8-22 type prosite sequence FRFGWSQAGFQSEMG description GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FrFGwSqAGFQsEmG source prosite : PS00653 54) chain B residue 76 type SITE sequence K description Not N6-methylated source Swiss-Prot : SWS_FT_FI3 55) chain B residue 102 type SITE sequence K description Not N6-methylated source Swiss-Prot : SWS_FT_FI3 56) chain B residue 124 type SITE sequence K description Not N6-methylated source Swiss-Prot : SWS_FT_FI3 57) chain B residue 138 type SITE sequence K description Not N6-methylated source Swiss-Prot : SWS_FT_FI3 58) chain A residue 76 type SITE sequence K description Not N6-methylated source Swiss-Prot : SWS_FT_FI3 59) chain A residue 102 type SITE sequence K description Not N6-methylated source Swiss-Prot : SWS_FT_FI3 60) chain A residue 124 type SITE sequence K description Not N6-methylated source Swiss-Prot : SWS_FT_FI3 61) chain A residue 138 type SITE sequence K description Not N6-methylated source Swiss-Prot : SWS_FT_FI3

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