eF-site ID 1pbg-B PDB Code 1pbg Chain B click to enlarge Title THE THREE-DIMENSIONAL STRUCTURE OF 6-PHOSPHO-BETA GALACTOSIDASE FROM LACTOCOCCUS LACTIS Classification HYDROLASE (GLYCOSYL HYDROLASE) Compound 6-PHOSPHO-BETA-D-GALACTOSIDASE Source null (LACG_LACLA) Sequence B:  MTKTLPKDFIFGGATAAYQAEGATHTDGKGPVAWDKYLED NYWYTAEPASDFYHKYPVDLELAEEYGVNGIRISIAWSRI FPTGYGEVNEKGVEFYHKLFAECHKRHVEPFVTLHHFDTP EALHSNGDFLNRENIEHFIDYAAFCFEEFPEVNYWTTFNE IGPIGDGQYLVGKFPPGIKYDLAKVFQSHHNMMVSHARAV KLYKDKGYKGEIGVVHALPTKYPYDPENPADVRAAELEDI IHNKFILDATYLGHYSDKTMEGVNHILAENGGELDLRDED FQALDAAKDLNDFLGINYYMSDWMQAFDGETEIIHSKYQI KGVGRRVAPDYVPRWIIYPEGLYDQIMRVKNDYPNYKKIY ITENGLGYKDEFVDNTVYDDGRIDYVKQHLEVLSDAIADG ANVKGYFIWSLMDVFSWSNGYEKRYGLFYVDFDTQERYPK KSAHWYKKLAETQVIE Description Functional site 1) chain B residue 428 type sequence S description BINDING SITE FOR RESIDUE SO4 B 469 source : AC2 2) chain B residue 430 type sequence S description BINDING SITE FOR RESIDUE SO4 B 469 source : AC2 3) chain B residue 431 type sequence N description BINDING SITE FOR RESIDUE SO4 B 469 source : AC2 4) chain B residue 437 type sequence Y description BINDING SITE FOR RESIDUE SO4 B 469 source : AC2 5) chain B residue 19 type BINDING sequence Q description BINDING => ECO:0000255|HAMAP-Rule:MF_01574, ECO:0000269|PubMed:9223646, ECO:0007744|PDB:4PBG source Swiss-Prot : SWS_FT_FI3 6) chain B residue 116 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_01574, ECO:0000269|PubMed:9223646, ECO:0007744|PDB:4PBG source Swiss-Prot : SWS_FT_FI3 7) chain B residue 159 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_01574, ECO:0000269|PubMed:9223646, ECO:0007744|PDB:4PBG source Swiss-Prot : SWS_FT_FI3 8) chain B residue 160 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_01574, ECO:0000269|PubMed:9223646, ECO:0007744|PDB:4PBG source Swiss-Prot : SWS_FT_FI3 9) chain B residue 297 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_01574, ECO:0000269|PubMed:9223646, ECO:0007744|PDB:4PBG source Swiss-Prot : SWS_FT_FI3 10) chain B residue 428 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_01574, ECO:0000269|PubMed:9223646, ECO:0007744|PDB:4PBG source Swiss-Prot : SWS_FT_FI3 11) chain B residue 429 type BINDING sequence W description BINDING => ECO:0000255|HAMAP-Rule:MF_01574, ECO:0000269|PubMed:9223646, ECO:0007744|PDB:4PBG source Swiss-Prot : SWS_FT_FI3 12) chain B residue 435 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_01574, ECO:0000269|PubMed:9223646, ECO:0007744|PDB:4PBG source Swiss-Prot : SWS_FT_FI3 13) chain B residue 437 type BINDING sequence Y description BINDING => ECO:0000255|HAMAP-Rule:MF_01574, ECO:0000269|PubMed:9223646, ECO:0007744|PDB:4PBG source Swiss-Prot : SWS_FT_FI3 14) chain B residue 160 type ACT_SITE sequence E description Proton donor => ECO:0000255|HAMAP-Rule:MF_01574, ECO:0000305|PubMed:8535789 source Swiss-Prot : SWS_FT_FI1 15) chain B residue 375 type ACT_SITE sequence E description Nucleophile => ECO:0000255|HAMAP-Rule:MF_01574, ECO:0000305|PubMed:8535789 source Swiss-Prot : SWS_FT_FI2 16) chain B residue 160 type catalytic sequence E description 877 source MCSA : MCSA2 17) chain B residue 375 type catalytic sequence E description 877 source MCSA : MCSA2

Display surface Download Links