eF-site ID 1uwt-AB PDB Code 1uwt Chain A, B click to enlarge Title Structure of beta-glycosidase from Sulfolobus solfataricus in complex with D-galactohydroximo-1,5-lactam Classification HYDROLASE Compound BETA-GALACTOSIDASE Source Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (BGAM_SULSO) Sequence A:  MYSFPNSFRFGWSQAGFQSEMGTPGSEDPNTDWYKWVHDP ENMAAGLVSGDLPENGPGYWGNYKTFHDNAQKMGLKIARL NVEWSRIFPNPLPRPFDESKQDVTEVEINENELKRLDEYA NKDALNHYREIFKDLKSRGLYFILNMYHWPLPLWLHDPIR VRRGDFTGPSGWLSTRTVYEFARFSAYIAWKFDDLVDEYS TMNEPNVVGGLGYVGVKSGFPPGYLSFELSRRAMYNIIQA HARAYDGIKSVSKKPVGIIYANSSFQPLTDKDMEAVEMAE NDNRWWFFDAIIRGEITREKIVRDDLKGRLDWIGVNYYTR TVVKRTEKGYVSLGGYGHGCERNSVSLAGLPTSDFGWEFF PEGLYDVLTKYWNRYHLYMYVTENGIADDADYQRPYYLVS HVYQVHRAINSGADVRGYLHWSLADNYEWASGFSMRFGLL KVDYNTKRLYWRPSALVYREIATNGAITDEIEHLNSVPPV KPLRH B:  MYSFPNSFRFGWSQAGFQSEMGTPGSEDPNTDWYKWVHDP ENMAAGLVSGDLPENGPGYWGNYKTFHDNAQKMGLKIARL NVEWSRIFPNPLPRPFDESKQDVTEVEINENELKRLDEYA NKDALNHYREIFKDLKSRGLYFILNMYHWPLPLWLHDPIR VRRGDFTGPSGWLSTRTVYEFARFSAYIAWKFDDLVDEYS TMNEPNVVGGLGYVGVKSGFPPGYLSFELSRRAMYNIIQA HARAYDGIKSVSKKPVGIIYANSSFQPLTDKDMEAVEMAE NDNRWWFFDAIIRGEITRKIVRDDLKGRLDWIGVNYYTRT VVKRTEKGYVSLGGYGHGCERNSVSLAGLPTSDFGWEFFP EGLYDVLTKYWNRYHLYMYVTENGIADDADYQRPYYLVSH VYQVHRAINSGADVRGYLHWSLADNYEWASGFSMRFGLLK VDYNTKRLYWRPSALVYREIATNGAITDEIEHLNSVPPVK PLRH Description Functional site 1) chain A residue 113 type sequence N description BINDING SITE FOR RESIDUE ACT B 1490 source : AC1 2) chain B residue 410 type sequence H description BINDING SITE FOR RESIDUE ACT B 1490 source : AC1 3) chain B residue 411 type sequence R description BINDING SITE FOR RESIDUE ACT B 1490 source : AC1 4) chain A residue 18 type sequence Q description BINDING SITE FOR RESIDUE GTL A 1490 source : AC2 5) chain A residue 150 type sequence H description BINDING SITE FOR RESIDUE GTL A 1490 source : AC2 6) chain A residue 205 type sequence N description BINDING SITE FOR RESIDUE GTL A 1490 source : AC2 7) chain A residue 206 type sequence E description BINDING SITE FOR RESIDUE GTL A 1490 source : AC2 8) chain A residue 322 type sequence Y description BINDING SITE FOR RESIDUE GTL A 1490 source : AC2 9) chain A residue 361 type sequence W description BINDING SITE FOR RESIDUE GTL A 1490 source : AC2 10) chain A residue 387 type sequence E description BINDING SITE FOR RESIDUE GTL A 1490 source : AC2 11) chain A residue 425 type sequence W description BINDING SITE FOR RESIDUE GTL A 1490 source : AC2 12) chain A residue 432 type sequence E description BINDING SITE FOR RESIDUE GTL A 1490 source : AC2 13) chain A residue 433 type sequence W description BINDING SITE FOR RESIDUE GTL A 1490 source : AC2 14) chain A residue 441 type sequence F description BINDING SITE FOR RESIDUE GTL A 1490 source : AC2 15) chain B residue 18 type sequence Q description BINDING SITE FOR RESIDUE GTL B 1491 source : AC3 16) chain B residue 150 type sequence H description BINDING SITE FOR RESIDUE GTL B 1491 source : AC3 17) chain B residue 205 type sequence N description BINDING SITE FOR RESIDUE GTL B 1491 source : AC3 18) chain B residue 206 type sequence E description BINDING SITE FOR RESIDUE GTL B 1491 source : AC3 19) chain B residue 322 type sequence Y description BINDING SITE FOR RESIDUE GTL B 1491 source : AC3 20) chain B residue 361 type sequence W description BINDING SITE FOR RESIDUE GTL B 1491 source : AC3 21) chain B residue 387 type sequence E description BINDING SITE FOR RESIDUE GTL B 1491 source : AC3 22) chain B residue 425 type sequence W description BINDING SITE FOR RESIDUE GTL B 1491 source : AC3 23) chain B residue 432 type sequence E description BINDING SITE FOR RESIDUE GTL B 1491 source : AC3 24) chain B residue 433 type sequence W description BINDING SITE FOR RESIDUE GTL B 1491 source : AC3 25) chain B residue 441 type sequence F description BINDING SITE FOR RESIDUE GTL B 1491 source : AC3 26) chain A residue 383-391 type prosite sequence MYVTENGIA description GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. MYVTENGIA source prosite : PS00572 27) 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 28) chain A residue 206 type ACT_SITE sequence E description Proton donor => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 29) chain B residue 206 type ACT_SITE sequence E description Proton donor => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 30) chain A residue 387 type ACT_SITE sequence E description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10055 source Swiss-Prot : SWS_FT_FI2 31) chain B residue 387 type ACT_SITE sequence E description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10055 source Swiss-Prot : SWS_FT_FI2 32) chain A residue 76 type SITE sequence K description Not N6-methylated source Swiss-Prot : SWS_FT_FI3 33) chain A residue 102 type SITE sequence K description Not N6-methylated source Swiss-Prot : SWS_FT_FI3 34) chain A residue 124 type SITE sequence K description Not N6-methylated source Swiss-Prot : SWS_FT_FI3 35) chain A residue 138 type SITE sequence K description Not N6-methylated source Swiss-Prot : SWS_FT_FI3 36) chain B residue 76 type SITE sequence K description Not N6-methylated source Swiss-Prot : SWS_FT_FI3 37) chain B residue 102 type SITE sequence K description Not N6-methylated source Swiss-Prot : SWS_FT_FI3 38) chain B residue 124 type SITE sequence K description Not N6-methylated source Swiss-Prot : SWS_FT_FI3 39) chain B residue 138 type SITE sequence K description Not N6-methylated source Swiss-Prot : SWS_FT_FI3 40) chain A residue 116 type MOD_RES sequence K description N6-methyllysine; partial => ECO:0000269|PubMed:14660666 source Swiss-Prot : SWS_FT_FI4 41) chain A residue 273 type MOD_RES sequence K description N6-methyllysine; partial => ECO:0000269|PubMed:14660666 source Swiss-Prot : SWS_FT_FI4 42) chain A residue 311 type MOD_RES sequence K description N6-methyllysine; partial => ECO:0000269|PubMed:14660666 source Swiss-Prot : SWS_FT_FI4 43) chain B residue 116 type MOD_RES sequence K description N6-methyllysine; partial => ECO:0000269|PubMed:14660666 source Swiss-Prot : SWS_FT_FI4 44) chain B residue 273 type MOD_RES sequence K description N6-methyllysine; partial => ECO:0000269|PubMed:14660666 source Swiss-Prot : SWS_FT_FI4 45) chain B residue 311 type MOD_RES sequence K description N6-methyllysine; partial => ECO:0000269|PubMed:14660666 source Swiss-Prot : SWS_FT_FI4 46) chain A residue 135 type MOD_RES sequence K description N6-methyllysine => ECO:0000269|PubMed:14660666 source Swiss-Prot : SWS_FT_FI5 47) chain A residue 332 type MOD_RES sequence K description N6-methyllysine => ECO:0000269|PubMed:14660666 source Swiss-Prot : SWS_FT_FI5 48) chain B residue 135 type MOD_RES sequence K description N6-methyllysine => ECO:0000269|PubMed:14660666 source Swiss-Prot : SWS_FT_FI5 49) chain B residue 332 type MOD_RES sequence K description N6-methyllysine => ECO:0000269|PubMed:14660666 source Swiss-Prot : SWS_FT_FI5

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