eF-site ID 6qxk-AB PDB Code 6qxk Chain A, B click to enlarge Title Human PIM1 bound to OX0999 Classification TRANSFERASE Compound Serine/threonine-protein kinase pim-1 Source (6QXK) Sequence A:  RKRRRHPS B:  ESQYQVGPLLGGFGSVYSGIRVSDNLPVAIKHVEKDRISD WGELPNGTRVPMEVVLLKKVSSGFSGVIRLLDWFERPDSF VLILERPEPVQDLFDFITERGALQEELARSFFWQVLEAVR HCHNCGVLHRDIKDENILIDLNRGELKLIDFGSGALLKDT VYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLYDMV CGDIPFEHDEEIIGGQVFFRQRVSSECQHLIRWCLALRPS DRPTFEEIQNHPWMQDVLLPQETAEIHLH Description Functional site 1) chain B residue 49 type sequence F description binding site for residue JKW B 401 source : AC1 2) chain B residue 52 type sequence V description binding site for residue JKW B 401 source : AC1 3) chain B residue 65 type sequence A description binding site for residue JKW B 401 source : AC1 4) chain B residue 67 type sequence K description binding site for residue JKW B 401 source : AC1 5) chain B residue 121 type sequence E description binding site for residue JKW B 401 source : AC1 6) chain B residue 126 type sequence V description binding site for residue JKW B 401 source : AC1 7) chain B residue 171 type sequence E description binding site for residue JKW B 401 source : AC1 8) chain B residue 172 type sequence N description binding site for residue JKW B 401 source : AC1 9) chain B residue 174 type sequence L description binding site for residue JKW B 401 source : AC1 10) chain B residue 186 type sequence D description binding site for residue JKW B 401 source : AC1 11) chain B residue 44-67 type prosite sequence LGGFGSVYSGIRVSDNLPVAIK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGGFGSVYsGirvsdnlp..........VAIK source prosite : PS00107 12) chain B residue 163-175 type prosite sequence VLHRDIKDENILI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDIKdeNILI source prosite : PS00108 13) chain B residue 128 type BINDING sequence D description BINDING => ECO:0000305|PubMed:15525646, ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862 source Swiss-Prot : SWS_FT_FI3 14) chain B residue 121 type BINDING sequence E description BINDING => ECO:0000305|PubMed:15525646, ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862 source Swiss-Prot : SWS_FT_FI3 15) chain B residue 67 type BINDING sequence K description BINDING => ECO:0000305|PubMed:15525646, ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862 source Swiss-Prot : SWS_FT_FI3 16) chain B residue 167 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 17) chain B residue 44 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 18) chain B residue 261 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:15657054 source Swiss-Prot : SWS_FT_FI6 19) chain B residue 98 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:15657054 source Swiss-Prot : SWS_FT_FI6

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