eF-site ID 4uxz-A PDB Code 4uxz Chain A click to enlarge Title Structure of delta7-DgkA-syn in 7.9 MAG to 2.18 angstrom resolution Classification TRANSFERASE Compound DIACYLGLYCEROL KINASE-DELTA 7 Source (KDGL_ECOLI) Sequence A:  TGFTRIIKAAGYSWKGLRAAWINEAAFRQEGVAVLLCVVI AAWLDVDAVTRVLLISSVMLVMIVELLNSAIEAVVDRIGS EYHELSGRAKDLGSAAVLIAIIDAVITWAILLWSHFG Description Functional site 1) chain A residue 33 type sequence Q description BINDING SITE FOR RESIDUE 79M C 1122 source : AC2 2) chain A residue 34 type sequence E description BINDING SITE FOR RESIDUE 79M C 1122 source : AC2 3) chain A residue 41 type sequence C description BINDING SITE FOR RESIDUE 79M C 1122 source : AC2 4) chain A residue 30 type sequence A description BINDING SITE FOR RESIDUE 79M D 1124 source : AC6 5) chain A residue 31 type sequence F description BINDING SITE FOR RESIDUE 79M D 1124 source : AC6 6) chain A residue 34 type sequence E description BINDING SITE FOR RESIDUE 79M D 1124 source : AC6 7) chain A residue 69 type sequence E description BINDING SITE FOR RESIDUE 79M D 1124 source : AC6 8) chain A residue 102 type sequence L description BINDING SITE FOR RESIDUE 79M D 1124 source : AC6 9) chain A residue 22 type sequence R description BINDING SITE FOR RESIDUE 79N A 1122 source : AC7 10) chain A residue 25 type sequence W description BINDING SITE FOR RESIDUE 79N A 1122 source : AC7 11) chain A residue 63 type sequence M description BINDING SITE FOR RESIDUE 79N A 1122 source : AC7 12) chain A residue 43 type sequence V description BINDING SITE FOR RESIDUE 79N A 1123 source : BC1 13) chain A residue 47 type sequence W description BINDING SITE FOR RESIDUE 79N A 1123 source : BC1 14) chain A residue 48 type sequence L description BINDING SITE FOR RESIDUE 79N A 1123 source : BC1 15) chain A residue 120 type sequence F description BINDING SITE FOR RESIDUE 79N A 1123 source : BC1 16) chain A residue 40 type sequence L description BINDING SITE FOR RESIDUE 79N A 1124 source : BC2 17) chain A residue 47 type sequence W description BINDING SITE FOR RESIDUE 79N A 1124 source : BC2 18) chain A residue 55 type sequence R description BINDING SITE FOR RESIDUE 79M A 1125 source : BC4 19) chain A residue 52 type sequence A description BINDING SITE FOR RESIDUE 79M A 1126 source : BC5 20) chain A residue 55 type sequence R description BINDING SITE FOR RESIDUE 79M A 1126 source : BC5 21) 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 22) 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 23) 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 24) 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 25) chain A residue 16 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI10 26) chain A residue 28 type BINDING sequence E description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI10 27) chain A residue 76 type BINDING sequence E description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI10 28) chain A residue 85 type BINDING sequence E description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI10 29) chain A residue 94 type BINDING sequence K description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI10 30) 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 31) 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 32) 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 33) 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 34) 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 35) 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 36) 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 37) chain A residue 69-94 type TOPO_DOM sequence ELLNSAIEAVVDRIGSEYHELSGRAK description Cytoplasmic => ECO:0000305|PubMed:8071224 source Swiss-Prot : SWS_FT_FI4 38) chain A residue 95-118 type TRANSMEM sequence DLGSAAVLIAIIDAVITWAILLWS description Helical => ECO:0000305|PubMed:8071224 source Swiss-Prot : SWS_FT_FI5 39) 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 40) chain A residue 69 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:26673816 source Swiss-Prot : SWS_FT_FI7 41) 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 42) chain A residue 69-80 type prosite sequence ELLNSAIEAVVD description DAGK_PROKAR Prokaryotic diacylglycerol kinase signature. ElLNSAIEavVD source prosite : PS01069

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