eF-site ID 4bzo-A PDB Code 4bzo Chain A click to enlarge Title Crystal structure of PIM1 in complex with a Pyrrolo-Pyrazinone inhibitor Classification TRANSFERASE Compound SERINE/THREONINE-PROTEIN KINASE PIM-1 Source Homo sapiens (Human) (PIM1_HUMAN) Sequence A:  PLESQYQVGPLLGSGGFGSVYSGIRVSDNLPVAIKHVEKD RISDWGELPNGTRVPMEVVLLKKVSSGFSGVIRLLDWFER PDSFVLILERPEPVQDLFDFITERGALQEELARSFFWQVL EAVRHCHNCGVLHRDIKDENILIDLNRGELKLIDFGSGAL LKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILL YDMVCGDIPFEHDEEIIRGQVFFRQRVSXECQHLIRWCLA LRPSDRPTFEEIQNHPWMQDVLLPQETAEIHLH Description (1)  SERINE/THREONINE-PROTEIN KINASE PIM-1 (E.C.2.7.11.1) Functional site 1) chain A residue 44 type sequence L description BINDING SITE FOR RESIDUE 676 A 1306 source : AC1 2) chain A residue 45 type sequence G description BINDING SITE FOR RESIDUE 676 A 1306 source : AC1 3) chain A residue 49 type sequence F description BINDING SITE FOR RESIDUE 676 A 1306 source : AC1 4) chain A residue 65 type sequence A description BINDING SITE FOR RESIDUE 676 A 1306 source : AC1 5) chain A residue 67 type sequence K description BINDING SITE FOR RESIDUE 676 A 1306 source : AC1 6) chain A residue 104 type sequence I description BINDING SITE FOR RESIDUE 676 A 1306 source : AC1 7) chain A residue 121 type sequence E description BINDING SITE FOR RESIDUE 676 A 1306 source : AC1 8) chain A residue 122 type sequence R description BINDING SITE FOR RESIDUE 676 A 1306 source : AC1 9) chain A residue 128 type sequence D description BINDING SITE FOR RESIDUE 676 A 1306 source : AC1 10) chain A residue 185 type sequence I description BINDING SITE FOR RESIDUE 676 A 1306 source : AC1 11) chain A residue 186 type sequence D description BINDING SITE FOR RESIDUE 676 A 1306 source : AC1 12) chain A 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 13) chain A residue 44 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 14) chain A residue 261 type MOD_RES sequence X description Phosphoserine => ECO:0000269|PubMed:15657054 source Swiss-Prot : SWS_FT_FI6 15) chain A residue 98 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:15657054 source Swiss-Prot : SWS_FT_FI6 16) chain A residue 44-67 type prosite sequence LGSGGFGSVYSGIRVSDNLPVAIK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGGFGSVYsGirvsdnlp..........VAIK source prosite : PS00107 17) chain A residue 163-175 type prosite sequence VLHRDIKDENILI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDIKdeNILI source prosite : PS00108 18) chain A 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 19) chain A 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 20) chain A 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

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