eF-site ID 2fyc-ABCD PDB Code 2fyc Chain A, B, C, D click to enlarge Title Crystal structure of the catalytic domain of bovine beta1,4-galactosyltransferase-I in complex with alpha-lactalbumin, Ca and UDP-galactose Classification TRANSFERASE Compound Alpha-lactalbumin Source Mus musculus (Mouse) (B4GT1_BOVIN) Sequence A:  TELTKCKVSHAIKDIDGYQGISLLEWACVLFHTSGYDTQA VVNDNGSTEYGLFQISDRFWCKSSEFPESENICGISCDKL LDDELDDDIACAKKILAIKGIDYWKAYKPMCSEKLEQWRC EKP B:  LTACPEESPLLVGPMLIEFNIPVDLKLVEQQNPKVKLGGR YTPMDCISPHKVAIIIPFRNRQEHLKYWLYYLHPILQRQQ LDYGIYVINQAGESMFNRAKLLNVGFKEALKDYDYNCFVF SDVDLIPMNDHNTYRCFSQPRHISVAMDKFGFSLPYVQYF GGVSALSKQQFLSINGFPNNYWGWGGEDDDIYNRLAFRGM SVSRPNAVIGKTRHIRHSRDKKNEPNPQRFDRIAHTKETM LSDGLNSLTYMVLEVQRYPLYTKITVDIGTPS C:  TELTKCKVSHAIKDIDGYQGISLLEWACVLFHTSGYDTQA VVNDNGSTEYGLFQISDRFWCKSSEFPESENICGISCDKL LDDELDDDIACAKKILAIKGIDYWKAYKPMCSEKLEQWRC EKP D:  LTACPEESPLLVGPMLIEFNIPVDLKLVEQQNPKVKLGGR YTPMDCISPHKVAIIIPFRNRQEHLKYWLYYLHPILQRQQ LDYGIYVINQAGESMFNRAKLLNVGFKEALKDYDYNCFVF SDVDLIPMNDHNTYRCFSQPRHISVAMDKFGFSLPYVQYF GGVSALSKQQFLSINGFPNNYWGWGGEDDDIYNRLAFRGM SVSRPNAVIGKTRHIRHSRDKKNEPNPQRFDRIAHTKETM LSDGLNSLTYMVLEVQRYPLYTKITVDIGTPS Description Functional site 1) chain B residue 187 type sequence P description BINDING SITE FOR RESIDUE GDU B 403 source : AC1 2) chain B residue 188 type sequence F description BINDING SITE FOR RESIDUE GDU B 403 source : AC1 3) chain B residue 189 type sequence R description BINDING SITE FOR RESIDUE GDU B 403 source : AC1 4) chain B residue 191 type sequence R description BINDING SITE FOR RESIDUE GDU B 403 source : AC1 5) chain B residue 226 type sequence F description BINDING SITE FOR RESIDUE GDU B 403 source : AC1 6) chain B residue 228 type sequence R description BINDING SITE FOR RESIDUE GDU B 403 source : AC1 7) chain B residue 252 type sequence D description BINDING SITE FOR RESIDUE GDU B 403 source : AC1 8) chain B residue 253 type sequence V description BINDING SITE FOR RESIDUE GDU B 403 source : AC1 9) chain B residue 254 type sequence D description BINDING SITE FOR RESIDUE GDU B 403 source : AC1 10) chain B residue 279 type sequence K description BINDING SITE FOR RESIDUE GDU B 403 source : AC1 11) chain B residue 292 type sequence G description BINDING SITE FOR RESIDUE GDU B 403 source : AC1 12) chain B residue 314 type sequence W description BINDING SITE FOR RESIDUE GDU B 403 source : AC1 13) chain B residue 315 type sequence G description BINDING SITE FOR RESIDUE GDU B 403 source : AC1 14) chain B residue 317 type sequence E description BINDING SITE FOR RESIDUE GDU B 403 source : AC1 15) chain B residue 318 type sequence D description BINDING SITE FOR RESIDUE GDU B 403 source : AC1 16) chain B residue 347 type sequence H description BINDING SITE FOR RESIDUE GDU B 403 source : AC1 17) chain B residue 350 type sequence D description BINDING SITE FOR RESIDUE GDU B 403 source : AC1 18) chain D residue 187 type sequence P description BINDING SITE FOR RESIDUE GDU D 528 source : AC2 19) chain D residue 188 type sequence F description BINDING SITE FOR RESIDUE GDU D 528 source : AC2 20) chain D residue 189 type sequence R description BINDING SITE FOR RESIDUE GDU D 528 source : AC2 21) chain D residue 191 type sequence R description BINDING SITE FOR RESIDUE GDU D 528 source : AC2 22) chain D residue 226 type sequence F description BINDING SITE FOR RESIDUE GDU D 528 source : AC2 23) chain D residue 228 type sequence R description BINDING SITE FOR RESIDUE GDU D 528 source : AC2 24) chain D residue 252 type sequence D description BINDING SITE FOR RESIDUE GDU D 528 source : AC2 25) chain D residue 253 type sequence V description BINDING SITE FOR RESIDUE GDU D 528 source : AC2 26) chain D residue 254 type sequence D description BINDING SITE FOR RESIDUE GDU D 528 source : AC2 27) chain D residue 279 type sequence K description BINDING SITE FOR RESIDUE GDU D 528 source : AC2 28) chain D residue 292 type sequence G description BINDING SITE FOR RESIDUE GDU D 528 source : AC2 29) chain D residue 314 type sequence W description BINDING SITE FOR RESIDUE GDU D 528 source : AC2 30) chain D residue 315 type sequence G description BINDING SITE FOR RESIDUE GDU D 528 source : AC2 31) chain D residue 317 type sequence E description BINDING SITE FOR RESIDUE GDU D 528 source : AC2 32) chain D residue 318 type sequence D description BINDING SITE FOR RESIDUE GDU D 528 source : AC2 33) chain D residue 347 type sequence H description BINDING SITE FOR RESIDUE GDU D 528 source : AC2 34) chain D residue 350 type sequence D description BINDING SITE FOR RESIDUE GDU D 528 source : AC2 35) chain D residue 353 type sequence N description BINDING SITE FOR RESIDUE GDU D 528 source : AC2 36) chain A residue 79 type sequence K description BINDING SITE FOR RESIDUE CA A 124 source : AC3 37) chain A residue 82 type sequence D description BINDING SITE FOR RESIDUE CA A 124 source : AC3 38) chain A residue 84 type sequence E description BINDING SITE FOR RESIDUE CA A 124 source : AC3 39) chain A residue 87 type sequence D description BINDING SITE FOR RESIDUE CA A 124 source : AC3 40) chain A residue 88 type sequence D description BINDING SITE FOR RESIDUE CA A 124 source : AC3 41) chain C residue 79 type sequence K description BINDING SITE FOR RESIDUE CA C 526 source : AC4 42) chain C residue 82 type sequence D description BINDING SITE FOR RESIDUE CA C 526 source : AC4 43) chain C residue 84 type sequence E description BINDING SITE FOR RESIDUE CA C 526 source : AC4 44) chain C residue 87 type sequence D description BINDING SITE FOR RESIDUE CA C 526 source : AC4 45) chain C residue 88 type sequence D description BINDING SITE FOR RESIDUE CA C 526 source : AC4 46) chain B residue 254 type sequence D description BINDING SITE FOR RESIDUE CA B 404 source : AC5 47) chain B residue 344 type sequence H description BINDING SITE FOR RESIDUE CA B 404 source : AC5 48) chain B residue 347 type sequence H description BINDING SITE FOR RESIDUE CA B 404 source : AC5 49) chain D residue 254 type sequence D description BINDING SITE FOR RESIDUE CA D 527 source : AC6 50) chain D residue 344 type sequence H description BINDING SITE FOR RESIDUE CA D 527 source : AC6 51) chain D residue 347 type sequence H description BINDING SITE FOR RESIDUE CA D 527 source : AC6 52) chain B residue 155 type sequence L description BINDING SITE FOR RESIDUE UDP B 405 source : AC7 53) chain B residue 159 type sequence E description BINDING SITE FOR RESIDUE UDP B 405 source : AC7 54) chain B residue 192 type sequence Q description BINDING SITE FOR RESIDUE UDP B 405 source : AC7 55) chain B residue 386 type sequence Q description BINDING SITE FOR RESIDUE UDP B 405 source : AC7 56) chain B residue 388 type sequence Y description BINDING SITE FOR RESIDUE UDP B 405 source : AC7 57) chain B residue 389 type sequence P description BINDING SITE FOR RESIDUE UDP B 405 source : AC7 58) chain B residue 390 type sequence L description BINDING SITE FOR RESIDUE UDP B 405 source : AC7 59) chain B residue 391 type sequence Y description BINDING SITE FOR RESIDUE UDP B 405 source : AC7 60) chain B residue 393 type sequence K description BINDING SITE FOR RESIDUE UDP B 405 source : AC7 61) chain D residue 155 type sequence L description BINDING SITE FOR RESIDUE UDP D 529 source : AC8 62) chain D residue 156 type sequence K description BINDING SITE FOR RESIDUE UDP D 529 source : AC8 63) chain D residue 159 type sequence E description BINDING SITE FOR RESIDUE UDP D 529 source : AC8 64) chain D residue 192 type sequence Q description BINDING SITE FOR RESIDUE UDP D 529 source : AC8 65) chain D residue 386 type sequence Q description BINDING SITE FOR RESIDUE UDP D 529 source : AC8 66) chain D residue 388 type sequence Y description BINDING SITE FOR RESIDUE UDP D 529 source : AC8 67) chain D residue 389 type sequence P description BINDING SITE FOR RESIDUE UDP D 529 source : AC8 68) chain D residue 390 type sequence L description BINDING SITE FOR RESIDUE UDP D 529 source : AC8 69) chain D residue 391 type sequence Y description BINDING SITE FOR RESIDUE UDP D 529 source : AC8 70) chain D residue 393 type sequence K description BINDING SITE FOR RESIDUE UDP D 529 source : AC8 71) chain A residue 49 type sequence E description BINDING SITE FOR RESIDUE MES A 805 source : AC9 72) chain A residue 54 type sequence Q description BINDING SITE FOR RESIDUE MES A 805 source : AC9 73) chain A residue 99 type sequence K description BINDING SITE FOR RESIDUE MES A 805 source : AC9 74) chain A residue 103 type sequence Y description BINDING SITE FOR RESIDUE MES A 805 source : AC9 75) chain A residue 105 type sequence K description BINDING SITE FOR RESIDUE MES A 805 source : AC9 76) chain B residue 325 type catalytic sequence L description 570 source MCSA : MCSA1 77) chain B residue 327 type catalytic sequence F description 570 source MCSA : MCSA1 78) chain B residue 387 type catalytic sequence R description 570 source MCSA : MCSA1 79) chain B residue 390 type catalytic sequence L description 570 source MCSA : MCSA1 80) chain B residue 391 type catalytic sequence Y description 570 source MCSA : MCSA1 81) chain D residue 325 type catalytic sequence L description 570 source MCSA : MCSA2 82) chain D residue 327 type catalytic sequence F description 570 source MCSA : MCSA2 83) chain D residue 387 type catalytic sequence R description 570 source MCSA : MCSA2 84) chain D residue 390 type catalytic sequence L description 570 source MCSA : MCSA2 85) chain D residue 391 type catalytic sequence Y description 570 source MCSA : MCSA2 86) 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 87) chain B residue 260 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 88) chain D residue 327 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI1 89) chain D residue 387 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 90) chain D residue 389 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 91) chain B residue 299 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI1 92) chain B residue 326 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI1 93) chain B residue 327 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI1 94) chain B residue 387 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 95) chain B residue 389 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 96) chain D residue 260 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 97) chain D residue 299 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI1 98) chain D residue 326 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI1 99) chain B residue 163 type CARBOHYD sequence P description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:2117606 source Swiss-Prot : SWS_FT_FI2 100) chain D residue 163 type CARBOHYD sequence P description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:2117606 source Swiss-Prot : SWS_FT_FI2 101) chain B residue 190 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 102) chain D residue 190 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3

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