eF-site ID 4uxx-B PDB Code 4uxx Chain B click to enlarge Title Structure of delta4-DgkA with AMPPCP in 9.9 MAG Classification TRANSFERASE Compound DIACYLGLYCEROL KINASE Source (KDGL_ECOLI) Sequence B:  GFTRIIKAAGYSWKGLRAAWINEAAFRQEGVAVLLAVVIA CWLDVDACTRVLLISSVMLVMIVELLNSAIEAVVDRIGSE YHELSGRAKDLGSAAVLIAIIDAVITWCILLWSHFG Description Functional site 1) chain B residue 9 type sequence R description BINDING SITE FOR RESIDUE ACP C 1123 source : AC4 2) chain B residue 16 type sequence Y description BINDING SITE FOR RESIDUE ACP C 1123 source : AC4 3) chain B residue 88 type sequence E description BINDING SITE FOR RESIDUE MPD B 1122 source : AC5 4) chain B residue 89 type sequence L description BINDING SITE FOR RESIDUE MPD B 1122 source : AC5 5) chain B residue 90 type sequence S description BINDING SITE FOR RESIDUE MPD B 1122 source : AC5 6) chain B residue 92 type sequence R description BINDING SITE FOR RESIDUE MPD B 1122 source : AC5 7) chain B residue 9 type sequence R description BINDING SITE FOR RESIDUE OLC C 1124 source : AC8 8) chain B residue 10 type sequence I description BINDING SITE FOR RESIDUE OLC C 1124 source : AC8 9) chain B residue 34 type sequence E description BINDING SITE FOR RESIDUE OLC B 1123 source : AC9 10) chain B residue 37 type sequence A description BINDING SITE FOR RESIDUE OLC B 1123 source : AC9 11) chain B residue 44 type sequence I description BINDING SITE FOR RESIDUE OLC B 1123 source : AC9 12) chain B residue 69 type sequence E description BINDING SITE FOR RESIDUE OLC B 1123 source : AC9 13) chain B residue 72 type sequence N description BINDING SITE FOR RESIDUE OLC B 1123 source : AC9 14) chain B residue 102 type sequence L description BINDING SITE FOR RESIDUE OLC B 1123 source : AC9 15) chain B residue 33 type sequence Q description BINDING SITE FOR RESIDUE OLC B 1124 source : BC1 16) chain B residue 34 type sequence E description BINDING SITE FOR RESIDUE OLC B 1124 source : BC1 17) chain B residue 112 type sequence W description BINDING SITE FOR RESIDUE OLC B 1124 source : BC1 18) chain B residue 117 type sequence W description BINDING SITE FOR RESIDUE OLC B 1124 source : BC1 19) chain B residue 39 type sequence L description BINDING SITE FOR RESIDUE OLC A 1125 source : BC3 20) chain B residue 40 type sequence L description BINDING SITE FOR RESIDUE OLC A 1125 source : BC3 21) chain B residue 47 type sequence W description BINDING SITE FOR RESIDUE OLC A 1125 source : BC3 22) chain B residue 13 type sequence A description BINDING SITE FOR RESIDUE OLC C 1125 source : BC4 23) chain B residue 17 type sequence S description BINDING SITE FOR RESIDUE OLC C 1125 source : BC4 24) chain B residue 76 type sequence E description BINDING SITE FOR RESIDUE ACT B 1125 source : BC5 25) chain B residue 83 type sequence G description BINDING SITE FOR RESIDUE ACT B 1125 source : BC5 26) chain B residue 84 type sequence S description BINDING SITE FOR RESIDUE ACT B 1125 source : BC5 27) chain B residue 85 type sequence E description BINDING SITE FOR RESIDUE ACT B 1125 source : BC5 28) chain B residue 86 type sequence Y description BINDING SITE FOR RESIDUE ACT B 1125 source : BC5 29) chain B residue 87 type sequence H description BINDING SITE FOR RESIDUE ACT B 1125 source : BC5 30) chain B residue 94 type sequence K description BINDING SITE FOR RESIDUE ACT B 1125 source : BC5 31) chain B residue 28 type sequence E description BINDING SITE FOR RESIDUE NA B 1126 source : BC6 32) chain B residue 76 type sequence E description BINDING SITE FOR RESIDUE NA B 1126 source : BC6 33) chain B residue 69 type BINDING sequence E description BINDING => ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI15 34) chain B residue 98 type BINDING sequence S description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129 source Swiss-Prot : SWS_FT_FI16 35) chain B residue 112 type BINDING sequence W description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI17 36) chain B residue 94 type BINDING sequence K description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI10 37) chain B residue 16 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI10 38) chain B residue 28 type BINDING sequence E description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI10 39) chain B residue 76 type BINDING sequence E description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI10 40) chain B residue 85 type BINDING sequence E description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI10 41) chain B residue 22 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26960129 source Swiss-Prot : SWS_FT_FI11 42) chain B residue 30 type BINDING sequence A description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129 source Swiss-Prot : SWS_FT_FI12 43) chain B residue 47 type BINDING sequence W description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.25 source Swiss-Prot : SWS_FT_FI13 44) chain B residue 55 type BINDING sequence R description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.25 source Swiss-Prot : SWS_FT_FI14 45) chain B residue 13 type BINDING sequence A description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129 source Swiss-Prot : SWS_FT_FI9 46) chain B residue 31-47 type TRANSMEM sequence FRQEGVAVLLAVVIACW description Helical => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224 source Swiss-Prot : SWS_FT_FI2 47) chain B residue 51-68 type TRANSMEM sequence DACTRVLLISSVMLVMIV description Helical => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224 source Swiss-Prot : SWS_FT_FI2 48) chain B residue 48-50 type TOPO_DOM sequence LDV description Periplasmic => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224 source Swiss-Prot : SWS_FT_FI3 49) chain B residue 69-94 type TOPO_DOM sequence ELLNSAIEAVVDRIGSEYHELSGRAK description Cytoplasmic => ECO:0000305|PubMed:8071224 source Swiss-Prot : SWS_FT_FI4 50) chain B residue 95-118 type TRANSMEM sequence DLGSAAVLIAIIDAVITWCILLWS description Helical => ECO:0000305|PubMed:8071224 source Swiss-Prot : SWS_FT_FI5 51) chain B residue 119-121 type TOPO_DOM sequence HFG description Periplasmic => ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:8071224 source Swiss-Prot : SWS_FT_FI6 52) chain B residue 69 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:26673816 source Swiss-Prot : SWS_FT_FI7 53) chain B residue 9 type BINDING sequence R description BINDING => ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538 source Swiss-Prot : SWS_FT_FI8

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