eF-site ID 1tw5-AB PDB Code 1tw5 Chain A, B click to enlarge Title beta1,4-galactosyltransferase mutant M344H-Gal-T1 in complex with Chitobiose Classification TRANSFERASE Compound Beta-1,4-galactosyltransferase 1 Source (B4GT1_BOVIN) Sequence A:  LTACPEESPLLVGPMLIEFNIPVDLKLVEQQNPKVKLGGR YTPMDCISPHKVAIIIPFRNRQEHLKYWLYYLHPILQRQQ LDYGIYVINQAGESMFNRAKLLNVGFKEALKDYDYNCFVF SDVDLIPMNDHNTYRCFSQPRHISVAMDKFGFSLPYVQYF GGVSALSKQQFLSINGFPNNYWGWGGEDDDIYNRLAFRGM SVSRPNAVIGKTRHIRHSRDKKNEPNPQRFDRIAHTKETM LSDGLNSLTYMVLEVQRYPLYTKITVDIGTPS B:  LTACPEESPLLVGPMLIEFNIPVDLKLVEQQNPKVKLGGR YTPMDCISPHKVAIIIPFRNRQEHLKYWLYYLHPILQRQQ LDYGIYVINQAGESMFNRAKLLNVGFKEALKDYDYNCFVF SDVDLIPMNDHNTYRCFSQPRHISVAMDKFGFSLPYVQYF GGVSALSKQQFLSINGFPNNYWGWGGEDDDIYNRLAFRGM SVSRPNAVIGKTRHIRHSRDKKNEPNPQRFDRIAHTKETM LSDGLNSLTYMVLEVQRYPLYTKITVDIGTPS Description Functional site 1) chain A residue 163 type CARBOHYD sequence P description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:2117606 source Swiss-Prot : SWS_FT_FI2 2) chain B residue 163 type CARBOHYD sequence P description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:2117606 source Swiss-Prot : SWS_FT_FI2 3) chain A residue 190 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 4) chain B residue 190 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 5) chain A residue 325 type catalytic sequence L description 570 source MCSA : MCSA1 6) chain A residue 327 type catalytic sequence F description 570 source MCSA : MCSA1 7) chain A residue 387 type catalytic sequence R description 570 source MCSA : MCSA1 8) chain A residue 390 type catalytic sequence L description 570 source MCSA : MCSA1 9) chain A residue 391 type catalytic sequence Y description 570 source MCSA : MCSA1 10) chain B residue 325 type catalytic sequence L description 570 source MCSA : MCSA2 11) chain B residue 327 type catalytic sequence F description 570 source MCSA : MCSA2 12) chain B residue 387 type catalytic sequence R description 570 source MCSA : MCSA2 13) chain B residue 390 type catalytic sequence L description 570 source MCSA : MCSA2 14) chain B residue 391 type catalytic sequence Y description 570 source MCSA : MCSA2 15) chain A residue 260 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 16) chain B residue 327 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI1 17) chain B residue 387 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 18) chain B residue 389 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 19) chain A residue 299 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI1 20) chain A residue 326 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI1 21) chain A residue 327 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI1 22) chain A residue 387 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 23) chain A residue 389 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 24) chain B residue 260 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 25) chain B residue 299 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI1 26) chain B residue 326 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI1

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