eF-site ID 1pbg-A PDB Code 1pbg Chain A 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 A:  MTKTLPKDFIFGGATAAYQAEGATHTDGKGPVAWDKYLED NYWYTAEPASDFYHKYPVDLELAEEYGVNGIRISIAWSRI FPTGYGEVNEKGVEFYHKLFAECHKRHVEPFVTLHHFDTP EALHSNGDFLNRENIEHFIDYAAFCFEEFPEVNYWTTFNE IGPIGDGQYLVGKFPPGIKYDLAKVFQSHHNMMVSHARAV KLYKDKGYKGEIGVVHALPTKYPYDPENPADVRAAELEDI IHNKFILDATYLGHYSDKTMEGVNHILAENGGELDLRDED FQALDAAKDLNDFLGINYYMSDWMQAFDGETEIIKYQIKG VGRRVAPDYVPRWIIYPEGLYDQIMRVKNDYPNYKKIYIT ENGLGYKDEFVDNTVYDDGRIDYVKQHLEVLSDAIADGAN VKGYFIWSLMDVFSWSNGYEKRYGLFYVDFDTQERYPKKS AHWYKKLAETQVIE Description Functional site 1) chain A residue 428 type sequence S description BINDING SITE FOR RESIDUE SO4 A 469 source : AC1 2) chain A residue 435 type sequence K description BINDING SITE FOR RESIDUE SO4 A 469 source : AC1 3) chain A 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 4) chain A 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 5) chain A 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 6) chain A 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 7) chain A 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 8) chain A 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 9) chain A 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 10) chain A 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 11) chain A 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 12) chain A 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 13) chain A 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 14) chain A residue 160 type catalytic sequence E description 877 source MCSA : MCSA1 15) chain A residue 375 type catalytic sequence E description 877 source MCSA : MCSA1 16) chain A residue 371-379 type prosite sequence IYITENGLG description GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. IYITENGLG source prosite : PS00572 17) chain A residue 9-23 type prosite sequence FIFGGATAAYQAEGA description GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FiFGgAtAAYQaEgA source prosite : PS00653

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