eF-site ID 5d57-A PDB Code 5d57 Chain A click to enlarge Title In meso X-ray crystallography structure of diacylglycerol kinase, DgkA, at 100 K Classification TRANSFERASE Compound Diacylglycerol kinase Source Escherichia coli (strain K12) (KDGL_ECOLI) Sequence A:  GFTRIIKAAGYSWKGLRAAWINEAAFRQEGVAVLLCVVIA AWLDVDAVTRVLLISSVMLVMIVELLNSAIEAVVDRIGSE YHELSGRAKDLGSAAVLIAIIDAVITWAILLWSHFG Description Functional site 1) chain A residue 46 type sequence A description binding site for residue 78M A 201 source : AC1 2) chain A residue 47 type sequence W description binding site for residue 78M A 201 source : AC1 3) chain A residue 49 type sequence D description binding site for residue 78M A 201 source : AC1 4) chain A residue 44 type sequence I description binding site for residue 78M A 202 source : AC2 5) chain A residue 120 type sequence F description binding site for residue 78M A 202 source : AC2 6) chain A residue 92 type sequence R description binding site for residue 78M A 203 source : AC3 7) chain A residue 95 type sequence D description binding site for residue 78M A 203 source : AC3 8) chain A residue 103 type sequence I description binding site for residue 78M A 203 source : AC3 9) chain A residue 18 type sequence W description binding site for residue 78M A 204 source : AC4 10) chain A residue 22 type sequence R description binding site for residue 78M A 204 source : AC4 11) chain A residue 25 type sequence W description binding site for residue 78M A 204 source : AC4 12) chain A residue 38 type sequence V description binding site for residue 78M A 204 source : AC4 13) chain A residue 39 type sequence L description binding site for residue 78M A 204 source : AC4 14) chain A residue 42 type sequence V description binding site for residue 78M A 204 source : AC4 15) chain A residue 63 type sequence M description binding site for residue 78M A 204 source : AC4 16) chain A residue 46 type sequence A description binding site for residue 78M A 205 source : AC5 17) chain A residue 55 type sequence R description binding site for residue 78M A 205 source : AC5 18) chain A residue 10 type sequence I description binding site for residue 78M A 206 source : AC6 19) chain A residue 13 type sequence A description binding site for residue 78M A 206 source : AC6 20) chain A residue 14 type sequence A description binding site for residue 78M A 206 source : AC6 21) chain A residue 17 type sequence S description binding site for residue 78M A 206 source : AC6 22) chain A residue 9 type sequence R description binding site for residue 78M B 202 source : AC8 23) chain A residue 116 type sequence L description binding site for residue 78M B 203 source : AC9 24) chain A residue 47 type sequence W description binding site for residue 78M C 201 source : AD2 25) chain A residue 40 type sequence L description binding site for residue 78M C 202 source : AD3 26) chain A residue 47 type sequence W description binding site for residue 78M C 202 source : AD3 27) chain A residue 117 type sequence W description binding site for residue 78M D 201 source : AD4 28) chain A residue 30 type sequence A description binding site for residue 78M D 202 source : AD5 29) chain A residue 31 type sequence F description binding site for residue 78M D 202 source : AD5 30) chain A residue 34 type sequence E description binding site for residue 78M D 202 source : AD5 31) chain A residue 69 type sequence E description binding site for residue 78M D 202 source : AD5 32) chain A residue 102 type sequence L description binding site for residue 78M D 202 source : AD5 33) chain A residue 105 type sequence I description binding site for residue 78M D 202 source : AD5 34) chain A residue 33 type sequence Q description binding site for residue 78M D 204 source : AD7 35) chain A residue 34 type sequence E description binding site for residue 78M D 204 source : AD7 36) chain A residue 37 type sequence A description binding site for residue 78M D 204 source : AD7 37) chain A residue 41 type sequence C description binding site for residue 78M D 204 source : AD7 38) 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 39) 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 40) 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 41) 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 42) chain A residue 69 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:26673816 source Swiss-Prot : SWS_FT_FI7 43) 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 44) 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 45) 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 46) 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 47) chain A residue 69-80 type prosite sequence ELLNSAIEAVVD description DAGK_PROKAR Prokaryotic diacylglycerol kinase signature. ElLNSAIEavVD source prosite : PS01069 48) 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 49) chain A residue 69-94 type TOPO_DOM sequence ELLNSAIEAVVDRIGSEYHELSGRAK description Cytoplasmic => ECO:0000305|PubMed:8071224 source Swiss-Prot : SWS_FT_FI4 50) chain A residue 95-118 type TRANSMEM sequence DLGSAAVLIAIIDAVITWAILLWS description Helical => ECO:0000305|PubMed:8071224 source Swiss-Prot : SWS_FT_FI5 51) 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 52) chain A residue 16 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI10 53) chain A residue 28 type BINDING sequence E description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI10 54) chain A residue 76 type BINDING sequence E description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI10 55) chain A residue 85 type BINDING sequence E description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI10 56) chain A residue 94 type BINDING sequence K description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI10 57) 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 58) 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 59) 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

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