eF-site ID 3ze3-A PDB Code 3ze3 Chain A click to enlarge Title Crystal structure of the integral membrane diacylglycerol kinase - delta7 Classification TRANSFERASE Compound DIACYLGLYCEROL KINASE Source (KDGL_ECOLI) Sequence A:  GFTRIIKAAGYSWKGLRAAWINEAAFRQEGVAVLLCVVIA AWLDVDAVTRVLLISSVMLVMIVELLNSAIEAVVDRIGSE YHELSGRAKDLGSAAVLIAIIDAVITWAILLWSHFG Description Functional site 1) chain A residue 13 type sequence A description BINDING SITE FOR RESIDUE 78N B 1122 source : AC6 2) chain A residue 14 type sequence A description BINDING SITE FOR RESIDUE 78N B 1122 source : AC6 3) chain A residue 17 type sequence S description BINDING SITE FOR RESIDUE 78N B 1122 source : AC6 4) chain A residue 9 type sequence R description BINDING SITE FOR RESIDUE 78N B 1123 source : AC7 5) chain A residue 33 type sequence Q description BINDING SITE FOR RESIDUE 78M D 1125 source : AC8 6) chain A residue 34 type sequence E description BINDING SITE FOR RESIDUE 78M D 1125 source : AC8 7) chain A residue 18 type sequence W description BINDING SITE FOR RESIDUE 78N A 1122 source : BC1 8) chain A residue 22 type sequence R description BINDING SITE FOR RESIDUE 78N A 1122 source : BC1 9) chain A residue 25 type sequence W description BINDING SITE FOR RESIDUE 78N A 1122 source : BC1 10) chain A residue 26 type sequence I description BINDING SITE FOR RESIDUE 78N A 1122 source : BC1 11) chain A residue 39 type sequence L description BINDING SITE FOR RESIDUE 78N A 1122 source : BC1 12) chain A residue 63 type sequence M description BINDING SITE FOR RESIDUE 78N A 1122 source : BC1 13) chain A residue 66 type sequence M description BINDING SITE FOR RESIDUE 78N A 1122 source : BC1 14) chain A residue 30 type sequence A description BINDING SITE FOR RESIDUE 78M D 1126 source : BC2 15) chain A residue 31 type sequence F description BINDING SITE FOR RESIDUE 78M D 1126 source : BC2 16) chain A residue 34 type sequence E description BINDING SITE FOR RESIDUE 78M D 1126 source : BC2 17) chain A residue 69 type sequence E description BINDING SITE FOR RESIDUE 78M D 1126 source : BC2 18) chain A residue 102 type sequence L description BINDING SITE FOR RESIDUE 78M D 1126 source : BC2 19) chain A residue 105 type sequence I description BINDING SITE FOR RESIDUE 78M D 1126 source : BC2 20) chain A residue 40 type sequence L description BINDING SITE FOR RESIDUE 78N C 1123 source : BC4 21) chain A residue 47 type sequence W description BINDING SITE FOR RESIDUE 78N C 1123 source : BC4 22) chain A residue 117 type sequence W description BINDING SITE FOR RESIDUE 78M D 1128 source : BC5 23) chain A residue 42 type sequence V description BINDING SITE FOR RESIDUE 78N A 1123 source : BC6 24) chain A residue 46 type sequence A description BINDING SITE FOR RESIDUE 78N A 1123 source : BC6 25) chain A residue 55 type sequence R description BINDING SITE FOR RESIDUE 78N A 1123 source : BC6 26) chain A residue 50 type sequence V description BINDING SITE FOR RESIDUE 78N A 1124 source : BC7 27) chain A residue 51 type sequence D description BINDING SITE FOR RESIDUE 78N A 1124 source : BC7 28) chain A residue 52 type sequence A description BINDING SITE FOR RESIDUE 78N A 1124 source : BC7 29) chain A residue 55 type sequence R description BINDING SITE FOR RESIDUE 78N A 1124 source : BC7 30) chain A residue 110 type sequence I description BINDING SITE FOR RESIDUE 78M A 1125 source : BC8 31) chain A residue 117 type sequence W description BINDING SITE FOR RESIDUE 78M A 1125 source : BC8 32) chain A residue 41 type sequence C description BINDING SITE FOR RESIDUE 78M A 1126 source : BC9 33) chain A residue 120 type sequence F description BINDING SITE FOR RESIDUE 78M A 1126 source : BC9 34) chain A 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 35) chain A residue 16 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI10 36) chain A residue 28 type BINDING sequence E description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI10 37) chain A residue 76 type BINDING sequence E description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI10 38) chain A residue 85 type BINDING sequence E description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI10 39) chain A residue 94 type BINDING sequence K description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI10 40) chain A 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 41) chain A 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 42) chain A 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 43) chain A 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 44) chain A residue 31-47 type TRANSMEM sequence FRQEGVAVLLCVVIAAW description Helical => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224 source Swiss-Prot : SWS_FT_FI2 45) chain A residue 51-68 type TRANSMEM sequence DAVTRVLLISSVMLVMIV description Helical => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224 source Swiss-Prot : SWS_FT_FI2 46) chain A residue 48-50 type TOPO_DOM sequence LDV description Periplasmic => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224 source Swiss-Prot : SWS_FT_FI3 47) chain A residue 69-94 type TOPO_DOM sequence ELLNSAIEAVVDRIGSEYHELSGRAK description Cytoplasmic => ECO:0000305|PubMed:8071224 source Swiss-Prot : SWS_FT_FI4 48) chain A residue 95-118 type TRANSMEM sequence DLGSAAVLIAIIDAVITWAILLWS description Helical => ECO:0000305|PubMed:8071224 source Swiss-Prot : SWS_FT_FI5 49) chain A residue 119-121 type TOPO_DOM sequence HFG description Periplasmic => ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:8071224 source Swiss-Prot : SWS_FT_FI6 50) chain A residue 69 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:26673816 source Swiss-Prot : SWS_FT_FI7 51) chain A residue 69-80 type prosite sequence ELLNSAIEAVVD description DAGK_PROKAR Prokaryotic diacylglycerol kinase signature. ElLNSAIEavVD source prosite : PS01069 52) chain A 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 53) chain A 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 54) chain A 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 55) chain A 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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