eF-site ID 1yxs-A PDB Code 1yxs Chain A click to enlarge Title Crystal Structure of Kinase Pim1 with P123M mutation Classification TRANSFERASE Compound Proto-oncogene serine/threonine-protein kinase Pim-1 Source null (PIM1_HUMAN) Sequence A:  PLESQYQVGPLLGSGGFGSVYSGIRVSDNLPVAIKHVEKD RISDWGELPNGTRVPMEVVLLKKVSSGFSGVIRLLDWFER PDSFVLILERMEPVQDLFDFITERGALQEELARSFFWQVL EAVRHCHNCGVLHRDIKDENILIDLNRGELKLIDFGSGAL LKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILL YDMVCGDIPFEHDEEIIRGQVFFRQRVSSECQHLIRWCLA LRPSDRPTFEEIQNHPWMQDVLLPQETAEIHLHS Description Functional site 1) chain A residue 130 type sequence F description BINDING SITE FOR RESIDUE IMD A 1001 source : AC1 2) chain A residue 133 type sequence I description BINDING SITE FOR RESIDUE IMD A 1001 source : AC1 3) chain A residue 134 type sequence T description BINDING SITE FOR RESIDUE IMD A 1001 source : AC1 4) chain A residue 170 type sequence D description BINDING SITE FOR RESIDUE IMD A 1001 source : AC1 5) chain A residue 234 type sequence D description BINDING SITE FOR RESIDUE IMD A 1001 source : AC1 6) chain A residue 238 type sequence G description BINDING SITE FOR RESIDUE IMD A 1001 source : AC1 7) chain A residue 239 type sequence D description BINDING SITE FOR RESIDUE IMD A 1001 source : AC1 8) 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 9) chain A residue 44 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 10) chain A residue 44-67 type prosite sequence LGSGGFGSVYSGIRVSDNLPVAIK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGGFGSVYsGirvsdnlp..........VAIK source prosite : PS00107 11) chain A residue 163-175 type prosite sequence VLHRDIKDENILI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDIKdeNILI source prosite : PS00108 12) 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 13) 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 14) 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 15) chain A residue 261 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:15657054 source Swiss-Prot : SWS_FT_FI4 16) chain A residue 98 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:15657054 source Swiss-Prot : SWS_FT_FI4

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