eF-site ID 3ber-A PDB Code 3ber Chain A click to enlarge Title Human DEAD-box RNA-helicase DDX47, conserved domain I in complex with AMP Classification HYDROLASE Compound Probable ATP-dependent RNA helicase DDX47 Source Homo sapiens (Human) (DDX47_HUMAN) Sequence A:  TEASQPIVEEEETKTFKDLGVTDVLCEACDQLGWTKPTKI QIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETP QRLFALVLTPTRELAFQISEQFEALGSSIGVQSAVIVGGI DSMSQSLALAKKPHIIIATPGRLIDHLENTKGFNLRALKY LVMDEADRILNMDFETEVDKILKVIPRDRKTFLFSATMTK KVQKLQRAALKNPVKCAVSS Description Functional site 1) chain A residue 128 type sequence G description BINDING SITE FOR RESIDUE PO4 A 350 source : AC1 2) chain A residue 129 type sequence G description BINDING SITE FOR RESIDUE PO4 A 350 source : AC1 3) chain A residue 151 type sequence G description BINDING SITE FOR RESIDUE PO4 A 350 source : AC1 4) chain A residue 152 type sequence R description BINDING SITE FOR RESIDUE PO4 A 350 source : AC1 5) chain A residue 155 type sequence D description BINDING SITE FOR RESIDUE PO4 A 350 source : AC1 6) chain A residue 26 type sequence F description BINDING SITE FOR RESIDUE AMP A 300 source : AC2 7) chain A residue 44 type sequence W description BINDING SITE FOR RESIDUE AMP A 300 source : AC2 8) chain A residue 46 type sequence K description BINDING SITE FOR RESIDUE AMP A 300 source : AC2 9) chain A residue 51 type sequence Q description BINDING SITE FOR RESIDUE AMP A 300 source : AC2 10) chain A residue 70 type sequence T description BINDING SITE FOR RESIDUE AMP A 300 source : AC2 11) chain A residue 71 type sequence G description BINDING SITE FOR RESIDUE AMP A 300 source : AC2 12) chain A residue 72 type sequence S description BINDING SITE FOR RESIDUE AMP A 300 source : AC2 13) chain A residue 73 type sequence G description BINDING SITE FOR RESIDUE AMP A 300 source : AC2 14) chain A residue 74 type sequence K description BINDING SITE FOR RESIDUE AMP A 300 source : AC2 15) chain A residue 75 type sequence T description BINDING SITE FOR RESIDUE AMP A 300 source : AC2 16) chain A residue 111 type sequence Q description BINDING SITE FOR RESIDUE AMP A 300 source : AC2 17) chain A residue 155 type sequence D description BINDING SITE FOR RESIDUE PGE A 400 source : AC3 18) chain A residue 155 type sequence D description BINDING SITE FOR RESIDUE PGE A 400 source : AC3 19) chain A residue 156 type sequence H description BINDING SITE FOR RESIDUE PGE A 400 source : AC3 20) chain A residue 156 type sequence H description BINDING SITE FOR RESIDUE PGE A 400 source : AC3 21) chain A residue 159 type sequence N description BINDING SITE FOR RESIDUE PGE A 400 source : AC3 22) chain A residue 159 type sequence N description BINDING SITE FOR RESIDUE PGE A 400 source : AC3 23) chain A residue 160 type sequence T description BINDING SITE FOR RESIDUE PGE A 400 source : AC3 24) chain A residue 160 type sequence T description BINDING SITE FOR RESIDUE PGE A 400 source : AC3 25) chain A residue 18 type sequence V description BINDING SITE FOR RESIDUE PGE A 401 source : AC4 26) chain A residue 192 type sequence L description BINDING SITE FOR RESIDUE PGE A 401 source : AC4 27) chain A residue 197 type sequence R description BINDING SITE FOR RESIDUE PGE A 401 source : AC4 28) chain A residue 199 type sequence R description BINDING SITE FOR RESIDUE PGE A 401 source : AC4 29) chain A residue 217 type sequence R description BINDING SITE FOR RESIDUE PGE A 401 source : AC4 30) chain A residue 218 type sequence A description BINDING SITE FOR RESIDUE PGE A 401 source : AC4 31) chain A residue 219 type sequence A description BINDING SITE FOR RESIDUE PGE A 401 source : AC4 32) chain A residue 220 type sequence L description BINDING SITE FOR RESIDUE PGE A 401 source : AC4 33) chain A residue 172-180 type prosite sequence VMDEADRIL description DEAD_ATP_HELICASE DEAD-box subfamily ATP-dependent helicases signature. VMDEADRiL source prosite : PS00039 34) chain A residue 68 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI1 35) chain A residue 149 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3

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