eF-site ID 3x03-A PDB Code 3x03 Chain A click to enlarge Title Crystal structure of PIP4KIIBETA complex with AMPPNP Classification TRANSFERASE Compound Phosphatidylinositol 5-phosphate 4-kinase type-2 beta Source Homo sapiens (Human) (PI42B_HUMAN) Sequence A:  KVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDF KAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFG IDDQDYQNSVTRSAPINSTRFLTTYDRRFVIKTVSSEDVA EMHNILKKYHQFIVECHGNTLLPQFLGMYRLTVDGVETYM VVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTF KDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMD YSLLVGIHDVDRAEQEEMEVEERAEDGPGEFDPSVDVYAM KSHESSPKKEVYFMAIIDILTVNPEQYSKRFNEFMSNILT Description Functional site 1) chain A residue 139 type sequence F description BINDING SITE FOR RESIDUE ANP A 501 source : AC1 2) chain A residue 148 type sequence V description BINDING SITE FOR RESIDUE ANP A 501 source : AC1 3) chain A residue 202 type sequence R description BINDING SITE FOR RESIDUE ANP A 501 source : AC1 4) chain A residue 203 type sequence N description BINDING SITE FOR RESIDUE ANP A 501 source : AC1 5) chain A residue 204 type sequence V description BINDING SITE FOR RESIDUE ANP A 501 source : AC1 6) chain A residue 214 type sequence K description BINDING SITE FOR RESIDUE ANP A 501 source : AC1 7) chain A residue 96 type sequence K description BINDING SITE FOR RESIDUE ANP A 502 source : AC2 8) chain A residue 98 type sequence Y description BINDING SITE FOR RESIDUE ANP A 502 source : AC2 9) chain A residue 154 type sequence S description BINDING SITE FOR RESIDUE ANP A 502 source : AC2 10) chain A residue 158 type sequence A description BINDING SITE FOR RESIDUE ANP A 502 source : AC2 11) chain A residue 161 type sequence H description BINDING SITE FOR RESIDUE ANP A 502 source : AC2 12) chain A residue 188 type sequence R description BINDING SITE FOR RESIDUE ANP A 502 source : AC2 13) chain A residue 195 type sequence E description BINDING SITE FOR RESIDUE ANP A 502 source : AC2 14) chain A residue 197 type sequence Y description BINDING SITE FOR RESIDUE ANP A 502 source : AC2 15) chain A residue 150 type catalytic sequence K description 662 source MCSA : MCSA1 16) chain A residue 278 type catalytic sequence D description 662 source MCSA : MCSA1 17) chain A residue 202 type BINDING sequence R description BINDING => ECO:0000305|PubMed:26774281, ECO:0007744|PDB:3X03 source Swiss-Prot : SWS_FT_FI1 18) chain A residue 203 type BINDING sequence N description BINDING => ECO:0000305|PubMed:26774281, ECO:0007744|PDB:3X04 source Swiss-Prot : SWS_FT_FI2 19) chain A residue 214 type BINDING sequence K description BINDING => ECO:0000305|PubMed:26774281, ECO:0007744|PDB:3X04 source Swiss-Prot : SWS_FT_FI2 20) chain A residue 369 type BINDING sequence D description BINDING => ECO:0000305|PubMed:26774281, ECO:0007744|PDB:3X04 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 94 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P48426 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 150 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4

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