eF-site ID 1nqi-ABCD PDB Code 1nqi Chain A, B, C, D click to enlarge Title crystal structure of lactose synthase, a 1:1 complex between beta1,4-galactosyltransferase and alpha-lactalbumin in the presence of GlcNAc Classification TRANSFERASE ACTIVATOR/TRANSFERASE Compound ALPHA-LACTALBUMIN Source (B4GT1_BOVIN) Sequence A:  TELTKCKVSHAIKDIDGYQGISLLEWACVLFHTSGYDTQA VVNDNGSTEYGLFQISDRFWCKSSEFPESENICGISCDKL LDDELDDDIACAKKILAIKGIDYWKAYKPMCSEKLEQWRC EKP B:  LTACPEESPLLVGPMLIEFNIPVDLKLVEQQNPKVKLGGR YTPMDCISPHKVAIIIPFRNRQEHLKYWLYYLHPILQRQQ LDYGIYVINQAGESMFNRAKLLNVGFKEALKDYDYNCFVF SDVDLIPMNDHNTYRCFSQPRHISVAMDKFGFSLPYVQYF GGVSALSKQQFLSINGFPNNYWGWGGEDDDIYNRLAFRGM SVSRPNAVIGKCRMIRHSRDKKNEPNPQRFDRIAHTKETM LSDGLNSLTYMVLEVQRYPLYTKITVDIGTPS C:  TELTKCKVSHAIKDIDGYQGISLLEWACVLFHTSGYDTQA VVNDNGSTEYGLFQISDRFWCKSSEFPESENICGISCDKL LDDELDDDIACAKKILAIKGIDYWKAYKPMCSEKLEQWRC EKP D:  LTACPEESPLLVGPMLIEFNIPVDLKLVEQQNPKVKLGGR YTPMDCISPHKVAIIIPFRNRQEHLKYWLYYLHPILQRQQ LDYGIYVINQAGESMFNRAKLLNVGFKEALKDYDYNCFVF SDVDLIPMNDHNTYRCFSQPRHISVAMDKFGFSLPYVQYF GGVSALSKQQFLSINGFPNNYWGWGGEDDDIYNRLAFRGM SVSRPNAVIGKCRMIRHSRDKKNEPNPQRFDRIAHTKETM LSDGLNSLTYMVLEVQRYPLYTKITVDIGTPS Description (1)  ALPHA-LACTALBUMIN, BETA-1,4-GALACTOSYLTRANSFERASE (E.C.2.4.1.22, E.C.2.4.1.90, E.C.2.4.1.38) Functional site 1) chain B residue 252 type catalytic sequence D description 570 source MCSA : MCSA1 2) chain B residue 254 type catalytic sequence D description 570 source MCSA : MCSA1 3) chain B residue 314 type catalytic sequence W description 570 source MCSA : MCSA1 4) chain B residue 317 type catalytic sequence E description 570 source MCSA : MCSA1 5) chain B residue 318 type catalytic sequence D description 570 source MCSA : MCSA1 6) chain B residue 344 type catalytic sequence M description 570 source MCSA : MCSA1 7) chain B residue 347 type catalytic sequence H description 570 source MCSA : MCSA1 8) chain B residue 349 type catalytic sequence R description 570 source MCSA : MCSA1 9) chain D residue 252 type catalytic sequence D description 570 source MCSA : MCSA2 10) chain D residue 254 type catalytic sequence D description 570 source MCSA : MCSA2 11) chain D residue 314 type catalytic sequence W description 570 source MCSA : MCSA2 12) chain D residue 317 type catalytic sequence E description 570 source MCSA : MCSA2 13) chain D residue 318 type catalytic sequence D description 570 source MCSA : MCSA2 14) chain D residue 344 type catalytic sequence M description 570 source MCSA : MCSA2 15) chain D residue 347 type catalytic sequence H description 570 source MCSA : MCSA2 16) chain D residue 349 type catalytic sequence R description 570 source MCSA : MCSA2 17) chain A residue 73-91 type prosite sequence CGISCDKLLDDELDDDIAC description GLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. CgisCdkLlddELdddiaC source prosite : PS00128 18) chain B residue 187 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 19) chain D residue 226 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI1 20) chain D residue 253 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI1 21) chain D residue 254 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 22) chain D residue 314 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI1 23) chain D residue 316 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI1 24) chain D residue 347 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 25) chain D residue 359 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 26) chain B residue 226 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI1 27) chain B residue 253 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI1 28) chain B residue 254 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 29) chain B residue 314 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI1 30) chain B residue 316 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI1 31) chain B residue 347 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI1 32) chain B residue 359 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 33) chain D residue 187 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 34) chain A residue 45 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 35) chain C residue 45 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI2

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