eF-site ID 1aky-A PDB Code 1aky Chain A click to enlarge Title HIGH-RESOLUTION STRUCTURES OF ADENYLATE KINASE FROM YEAST LIGATED WITH INHIBITOR AP5A, SHOWING THE PATHWAY OF PHOSPHORYL TRANSFER Classification TRANSFERASE (PHOSPHOTRANSFERASE) Compound ADENYLATE KINASE Source null (KAD1_YEAST) Sequence A:  ESIRMVLIGPPGAGKGTQAPNLQERFHAAHLATGDMLRSQ IAKGTQLGLEAKKIMDQGGLVSDDIMVNMIKDELTNNPAC KNGFILDGFPRTIPQAEKLDQMLKEQGTPLEKAIELKVDD ELLVARITGRLIHPASGRSYHKIFNPPKEDMKDDVTGEAL VQRSDDNADALKKRLAAYHAQTEPIVDFYKKTGIWAGVDA SQPPATVWADILNKLGKN Description Functional site 1) chain A residue 13 type sequence P description BINDING SITE FOR RESIDUE AP5 A 301 source : AC1 2) chain A residue 14 type sequence G description BINDING SITE FOR RESIDUE AP5 A 301 source : AC1 3) chain A residue 15 type sequence A description BINDING SITE FOR RESIDUE AP5 A 301 source : AC1 4) chain A residue 16 type sequence G description BINDING SITE FOR RESIDUE AP5 A 301 source : AC1 5) chain A residue 17 type sequence K description BINDING SITE FOR RESIDUE AP5 A 301 source : AC1 6) chain A residue 18 type sequence G description BINDING SITE FOR RESIDUE AP5 A 301 source : AC1 7) chain A residue 19 type sequence T description BINDING SITE FOR RESIDUE AP5 A 301 source : AC1 8) chain A residue 35 type sequence T description BINDING SITE FOR RESIDUE AP5 A 301 source : AC1 9) chain A residue 36 type sequence G description BINDING SITE FOR RESIDUE AP5 A 301 source : AC1 10) chain A residue 40 type sequence R description BINDING SITE FOR RESIDUE AP5 A 301 source : AC1 11) chain A residue 57 type sequence M description BINDING SITE FOR RESIDUE AP5 A 301 source : AC1 12) chain A residue 61 type sequence G description BINDING SITE FOR RESIDUE AP5 A 301 source : AC1 13) chain A residue 63 type sequence V description BINDING SITE FOR RESIDUE AP5 A 301 source : AC1 14) chain A residue 68 type sequence M description BINDING SITE FOR RESIDUE AP5 A 301 source : AC1 15) chain A residue 90 type sequence G description BINDING SITE FOR RESIDUE AP5 A 301 source : AC1 16) chain A residue 91 type sequence F description BINDING SITE FOR RESIDUE AP5 A 301 source : AC1 17) chain A residue 93 type sequence R description BINDING SITE FOR RESIDUE AP5 A 301 source : AC1 18) chain A residue 97 type sequence Q description BINDING SITE FOR RESIDUE AP5 A 301 source : AC1 19) chain A residue 128 type sequence R description BINDING SITE FOR RESIDUE AP5 A 301 source : AC1 20) chain A residue 132 type sequence R description BINDING SITE FOR RESIDUE AP5 A 301 source : AC1 21) chain A residue 141 type sequence S description BINDING SITE FOR RESIDUE AP5 A 301 source : AC1 22) chain A residue 142 type sequence Y description BINDING SITE FOR RESIDUE AP5 A 301 source : AC1 23) chain A residue 143 type sequence H description BINDING SITE FOR RESIDUE AP5 A 301 source : AC1 24) chain A residue 147 type sequence N description BINDING SITE FOR RESIDUE AP5 A 301 source : AC1 25) chain A residue 165 type sequence R description BINDING SITE FOR RESIDUE AP5 A 301 source : AC1 26) chain A residue 176 type sequence R description BINDING SITE FOR RESIDUE AP5 A 301 source : AC1 27) chain A residue 204 type sequence Q description BINDING SITE FOR RESIDUE AP5 A 301 source : AC1 28) chain A residue 205 type sequence P description BINDING SITE FOR RESIDUE AP5 A 301 source : AC1 29) chain A residue 206 type sequence P description BINDING SITE FOR RESIDUE AP5 A 301 source : AC1 30) chain A residue 18 type sequence G description BINDING SITE FOR RESIDUE IMD A 302 source : AC2 31) chain A residue 37 type sequence D description BINDING SITE FOR RESIDUE IMD A 302 source : AC2 32) chain A residue 40 type sequence R description BINDING SITE FOR RESIDUE IMD A 302 source : AC2 33) chain A residue 89 type sequence D description BINDING SITE FOR RESIDUE IMD A 302 source : AC2 34) chain A residue 14 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369, ECO:0000269|PubMed:8594191 source Swiss-Prot : SWS_FT_FI1 35) chain A residue 132 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369, ECO:0000269|PubMed:8594191 source Swiss-Prot : SWS_FT_FI1 36) chain A residue 204 type BINDING sequence Q description BINDING => ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369, ECO:0000269|PubMed:8594191 source Swiss-Prot : SWS_FT_FI1 37) chain A residue 35 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369 source Swiss-Prot : SWS_FT_FI2 38) chain A residue 40 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369 source Swiss-Prot : SWS_FT_FI2 39) chain A residue 61 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369 source Swiss-Prot : SWS_FT_FI2 40) chain A residue 90 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369 source Swiss-Prot : SWS_FT_FI2 41) chain A residue 97 type BINDING sequence Q description BINDING => ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369 source Swiss-Prot : SWS_FT_FI2 42) chain A residue 165 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369 source Swiss-Prot : SWS_FT_FI2 43) chain A residue 176 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369 source Swiss-Prot : SWS_FT_FI2 44) chain A residue 141 type BINDING sequence S description BINDING => ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369, ECO:0000269|PubMed:8594191 source Swiss-Prot : SWS_FT_FI3 45) chain A residue 86-97 type prosite sequence FILDGFPRTIPQ description ADENYLATE_KINASE Adenylate kinase signature. FILDGFPRtipQ source prosite : PS00113

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