eF-site ID 4uyo-D PDB Code 4uyo Chain D click to enlarge Title Structure of delta7-DgkA in 7.9 MAG by serial femtosecond crystatallography to 2.18 angstrom resolution Classification TRANSFERASE Compound DIACYLGLYCEROL KINASE-DELTA 7 Source (KDGL_ECOLI) Sequence D:  AGYSWKGLRAAWINEAAFRQEGVAVLLCVVIAAWLDVDAV TRVLLISSVMLVMIVELLNSAIEAVVDRIGSEYHELSGRA KDLGSAAVLIAIIDAVITWAILLWSHFG Description Functional site 1) chain D residue 33 type sequence Q description BINDING SITE FOR RESIDUE 79M B 1122 source : AC2 2) chain D residue 33 type sequence Q description BINDING SITE FOR RESIDUE 79M B 1124 source : AC4 3) chain D residue 34 type sequence E description BINDING SITE FOR RESIDUE 79M B 1124 source : AC4 4) chain D residue 105 type sequence I description BINDING SITE FOR RESIDUE 79M B 1124 source : AC4 5) chain D residue 109 type sequence V description BINDING SITE FOR RESIDUE 79M B 1124 source : AC4 6) chain D residue 25 type sequence W description BINDING SITE FOR RESIDUE 79N D 1123 source : AC6 7) chain D residue 29 type sequence A description BINDING SITE FOR RESIDUE 79N D 1123 source : AC6 8) chain D residue 32 type sequence R description BINDING SITE FOR RESIDUE 79N D 1123 source : AC6 9) chain D residue 36 type sequence V description BINDING SITE FOR RESIDUE 79N D 1123 source : AC6 10) chain D residue 47 type sequence W description BINDING SITE FOR RESIDUE 79N D 1124 source : AC7 11) chain D residue 48 type sequence L description BINDING SITE FOR RESIDUE 79N D 1124 source : AC7 12) chain D residue 49 type sequence D description BINDING SITE FOR RESIDUE 79N D 1124 source : AC7 13) chain D residue 120 type sequence F description BINDING SITE FOR RESIDUE 79N D 1124 source : AC7 14) chain D residue 25 type sequence W description BINDING SITE FOR RESIDUE 79M D 1125 source : AC8 15) chain D residue 39 type sequence L description BINDING SITE FOR RESIDUE 79M D 1125 source : AC8 16) chain D residue 28 type sequence E description BINDING SITE FOR RESIDUE ZN D 1122 source : BC1 17) chain D residue 76 type sequence E description BINDING SITE FOR RESIDUE ZN D 1122 source : BC1 18) chain D residue 28 type sequence E description BINDING SITE FOR RESIDUE FLC D 1126 source : BC2 19) chain D residue 76 type sequence E description BINDING SITE FOR RESIDUE FLC D 1126 source : BC2 20) 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 21) 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 22) 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 23) chain D residue 95-118 type TRANSMEM sequence DLGSAAVLIAIIDAVITWAILLWS description Helical => ECO:0000305|PubMed:8071224 source Swiss-Prot : SWS_FT_FI5 24) chain D residue 16 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI10 25) chain D residue 28 type BINDING sequence E description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI10 26) chain D residue 76 type BINDING sequence E description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI10 27) chain D residue 85 type BINDING sequence E description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI10 28) chain D residue 94 type BINDING sequence K description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26 source Swiss-Prot : SWS_FT_FI10 29) 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 30) 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 31) 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 32) 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 33) chain D residue 69-94 type TOPO_DOM sequence ELLNSAIEAVVDRIGSEYHELSGRAK description Cytoplasmic => ECO:0000305|PubMed:8071224 source Swiss-Prot : SWS_FT_FI4 34) chain D residue 69 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:26673816 source Swiss-Prot : SWS_FT_FI7 35) 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 36) 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 37) 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 38) 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

Display surface Download Links