eF-site ID 4ijp-AB PDB Code 4ijp Chain A, B click to enlarge Title Crystal Structure of Human PRPF4B kinase domain in complex with 4-{5-[(2-Chloro-pyridin-4-ylmethyl)-carbamoyl]-thiophen-2-yl}-benzo[b]thiophene-2-carboxylic acid amine Classification TRANSFERASE/TRANSFERASE INHIBITOR Compound Serine/threonine-protein kinase PRP4 homolog Source Homo sapiens (Human) (PRP4B_HUMAN) Sequence A:  DAEGYYRVNIGEVLDKRYNVYGYTGQGVFSNVVRARDNAR ANQEVAVKIIRNNELMQKTGLKELEFLKKLNDADPDDKFH CLRLFRHFYHKQHLCLVFEPLSMNLREVLKKYGKDVGLHI KAVRSYSQQLFLALKLLKRCNILHADIKPDNILVNESKTI LKLCDFGSASHVADNDITPXLVSRFYRAPEIIIGKSYDYG IDMWSVGCTLYELYTGKILFPGKTNNHMLKLAMDLKGKMP NKMIRKGVFKDQHFDQNLNFMYIEVDEREKVTVMSTINPT KDLLADLIQRLPEDQRKKVHQLKDLLDQILMLDPAKRISI NQALQHAFIQE B:  WTDAEGYYRVNIGEVLDKRYNVYGYTGQGVFSNVVRARDN ARANQEVAVKIIRNNELMQKTGLKELEFLKKLNDADPDDK FHCLRLFRHFYHKQHLCLVFEPLSMNLREVLKKYGKDVGL HIKAVRSYSQQLFLALKLLKRCNILHADIKPDNILVNESK TILKLCDFGSASHVADNDITPXLVSRFYRAPEIIIGKSYD YGIDMWSVGCTLYELYTGKILFPGKTNNHMLKLAMDLKGK MPNKMIRKGVFKDQHFDQNLNFMYIEVDREKVTVMSTINP TKDLLADLIGCQRLPEDQRKKVHQLKDLLDQILMLDPAKR ISINQALQHAFIQE Description (1)  Serine/threonine-protein kinase PRP4 homolog (E.C.2.7.11.1) Functional site 1) chain A residue 693 type sequence T description BINDING SITE FOR RESIDUE 1EH A 1101 source : AC1 2) chain A residue 701 type sequence V description BINDING SITE FOR RESIDUE 1EH A 1101 source : AC1 3) chain A residue 703 type sequence R description BINDING SITE FOR RESIDUE 1EH A 1101 source : AC1 4) chain A residue 715 type sequence A description BINDING SITE FOR RESIDUE 1EH A 1101 source : AC1 5) chain A residue 717 type sequence K description BINDING SITE FOR RESIDUE 1EH A 1101 source : AC1 6) chain A residue 768 type sequence E description BINDING SITE FOR RESIDUE 1EH A 1101 source : AC1 7) chain A residue 770 type sequence L description BINDING SITE FOR RESIDUE 1EH A 1101 source : AC1 8) chain A residue 771 type sequence S description BINDING SITE FOR RESIDUE 1EH A 1101 source : AC1 9) chain A residue 772 type sequence M description BINDING SITE FOR RESIDUE 1EH A 1101 source : AC1 10) chain A residue 776 type sequence E description BINDING SITE FOR RESIDUE 1EH A 1101 source : AC1 11) chain A residue 822 type sequence L description BINDING SITE FOR RESIDUE 1EH A 1101 source : AC1 12) chain A residue 686 type sequence R description BINDING SITE FOR RESIDUE SO4 A 1102 source : AC2 13) chain A residue 709 type sequence R description BINDING SITE FOR RESIDUE SO4 A 1102 source : AC2 14) chain B residue 709 type sequence R description BINDING SITE FOR RESIDUE SO4 A 1102 source : AC2 15) chain A residue 849 type sequence X description BINDING SITE FOR RESIDUE SO4 A 1103 source : AC3 16) chain A residue 853 type sequence R description BINDING SITE FOR RESIDUE SO4 A 1103 source : AC3 17) chain A residue 856 type sequence R description BINDING SITE FOR RESIDUE SO4 A 1103 source : AC3 18) chain A residue 804 type sequence K description BINDING SITE FOR RESIDUE SO4 A 1104 source : AC4 19) chain A residue 808 type sequence R description BINDING SITE FOR RESIDUE SO4 A 1104 source : AC4 20) chain B residue 990 type sequence K description BINDING SITE FOR RESIDUE SO4 A 1104 source : AC4 21) chain A residue 747 type sequence K description BINDING SITE FOR RESIDUE SO4 A 1105 source : AC5 22) chain A residue 748 type sequence F description BINDING SITE FOR RESIDUE SO4 A 1105 source : AC5 23) chain A residue 808 type sequence R description BINDING SITE FOR RESIDUE SO4 A 1105 source : AC5 24) chain B residue 693 type sequence T description BINDING SITE FOR RESIDUE 1EH B 1101 source : AC6 25) chain B residue 701 type sequence V description BINDING SITE FOR RESIDUE 1EH B 1101 source : AC6 26) chain B residue 703 type sequence R description BINDING SITE FOR RESIDUE 1EH B 1101 source : AC6 27) chain B residue 715 type sequence A description BINDING SITE FOR RESIDUE 1EH B 1101 source : AC6 28) chain B residue 717 type sequence K description BINDING SITE FOR RESIDUE 1EH B 1101 source : AC6 29) chain B residue 770 type sequence L description BINDING SITE FOR RESIDUE 1EH B 1101 source : AC6 30) chain B residue 771 type sequence S description BINDING SITE FOR RESIDUE 1EH B 1101 source : AC6 31) chain B residue 772 type sequence M description BINDING SITE FOR RESIDUE 1EH B 1101 source : AC6 32) chain B residue 776 type sequence E description BINDING SITE FOR RESIDUE 1EH B 1101 source : AC6 33) chain B residue 822 type sequence L description BINDING SITE FOR RESIDUE 1EH B 1101 source : AC6 34) chain B residue 849 type sequence X description BINDING SITE FOR RESIDUE SO4 B 1102 source : AC7 35) chain B residue 853 type sequence R description BINDING SITE FOR RESIDUE SO4 B 1102 source : AC7 36) chain B residue 856 type sequence R description BINDING SITE FOR RESIDUE SO4 B 1102 source : AC7 37) chain B residue 804 type sequence K description BINDING SITE FOR RESIDUE SO4 B 1103 source : AC8 38) chain B residue 808 type sequence R description BINDING SITE FOR RESIDUE SO4 B 1103 source : AC8 39) chain A residue 852 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q5RKH1 source Swiss-Prot : SWS_FT_FI5 40) chain B residue 852 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q5RKH1 source Swiss-Prot : SWS_FT_FI5 41) chain A residue 815 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 42) chain B residue 815 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 43) chain A residue 693 type BINDING sequence T description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 44) chain A residue 717 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 45) chain B residue 693 type BINDING sequence T description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 46) chain B residue 717 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 47) chain A residue 717 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 48) chain B residue 717 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 49) chain A residue 849 type MOD_RES sequence X description Phosphotyrosine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI4 50) chain B residue 849 type MOD_RES sequence X description Phosphotyrosine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI4 51) chain A residue 811-823 type prosite sequence ILHADIKPDNILV description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IlHaDIKpdNILV source prosite : PS00108

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