eF-site ID 5d57-D PDB Code 5d57 Chain D 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 D:  AGYSWKGLRAAWINEAAFRQEGVAVLLCVVIAAWLDVDAV TRVLLISSVMLVMIVELLNSAIEAVVDRIGSEYHELSGRA KDLGSAAVLIAIIDAVITWAILLWSHFG Description Functional site 1) chain D residue 39 type sequence L description binding site for residue 78M A 202 source : AC2 2) chain D residue 18 type sequence W description binding site for residue 78M A 203 source : AC3 3) chain D residue 36 type sequence V description binding site for residue 78M B 203 source : AC9 4) chain D residue 37 type sequence A description binding site for residue 78M B 203 source : AC9 5) chain D residue 102 type sequence L description binding site for residue 78M B 204 source : AD1 6) chain D residue 105 type sequence I description binding site for residue 78M B 204 source : AD1 7) chain D residue 46 type sequence A description binding site for residue 78M D 201 source : AD4 8) chain D residue 55 type sequence R description binding site for residue 78M D 201 source : AD4 9) chain D residue 59 type sequence I description binding site for residue 78M D 201 source : AD4 10) chain D residue 21 type sequence L description binding site for residue 78M D 202 source : AD5 11) chain D residue 22 type sequence R description binding site for residue 78M D 202 source : AD5 12) chain D residue 25 type sequence W description binding site for residue 78M D 202 source : AD5 13) chain D residue 26 type sequence I description binding site for residue 78M D 202 source : AD5 14) chain D residue 63 type sequence M description binding site for residue 78M D 202 source : AD5 15) chain D residue 47 type sequence W description binding site for residue 78M D 203 source : AD6 16) chain D residue 48 type sequence L description binding site for residue 78M D 203 source : AD6 17) chain D residue 49 type sequence D description binding site for residue 78M D 203 source : AD6 18) chain D residue 120 type sequence F description binding site for residue 78M D 203 source : AD6 19) chain D residue 32 type sequence R description binding site for residue 78M D 204 source : AD7 20) chain D residue 33 type sequence Q description binding site for residue 78M D 204 source : AD7 21) chain D residue 36 type sequence V description binding site for residue 78M D 204 source : AD7 22) chain D 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 23) chain D 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 24) chain D 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 25) chain D 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 26) chain D 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 27) chain D residue 16 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI10 28) chain D residue 28 type BINDING sequence E description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI10 29) chain D residue 76 type BINDING sequence E description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI10 30) chain D residue 85 type BINDING sequence E description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI10 31) chain D residue 94 type BINDING sequence K description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI10 32) chain D 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 33) chain D 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 34) chain D residue 31-47 type TRANSMEM sequence FRQEGVAVLLCVVIAAW description Helical => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224 source Swiss-Prot : SWS_FT_FI2 35) chain D residue 51-68 type TRANSMEM sequence DAVTRVLLISSVMLVMIV description Helical => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224 source Swiss-Prot : SWS_FT_FI2 36) chain D residue 48-50 type TOPO_DOM sequence LDV description Periplasmic => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224 source Swiss-Prot : SWS_FT_FI3 37) chain D residue 69-94 type TOPO_DOM sequence ELLNSAIEAVVDRIGSEYHELSGRAK description Cytoplasmic => ECO:0000305|PubMed:8071224 source Swiss-Prot : SWS_FT_FI4 38) chain D residue 95-118 type TRANSMEM sequence DLGSAAVLIAIIDAVITWAILLWS description Helical => ECO:0000305|PubMed:8071224 source Swiss-Prot : SWS_FT_FI5 39) chain D residue 119-121 type TOPO_DOM sequence HFG description Periplasmic => ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:8071224 source Swiss-Prot : SWS_FT_FI6 40) chain D residue 69 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:26673816 source Swiss-Prot : SWS_FT_FI7

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