eF-site ID 1fq1-B PDB Code 1fq1 Chain B click to enlarge Title CRYSTAL STRUCTURE OF KINASE ASSOCIATED PHOSPHATASE (KAP) IN COMPLEX WITH PHOSPHO-CDK2 Classification Hydrolase/Transferase Compound CYCLIN-DEPENDENT KINASE INHIBITOR 3 Source null (CDK2_HUMAN) Sequence B:  MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTE TEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVF EFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYX HEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRR ALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAA LAHPFFQDVTKPVPHL Description (1)  KINASE ASSOCIATED PHOSPHATASE (KAP) (E.C. 3.1.3.48)(C140S MUTANT) IN COMPLEX WITH PHOSPHO-CDK2 (E.C. 2.7.11.22) Functional site 1) chain B residue 132 type sequence N description BINDING SITE FOR RESIDUE MG B 383 source : AC1 2) chain B residue 145 type sequence D description BINDING SITE FOR RESIDUE MG B 383 source : AC1 3) chain B residue 10 type sequence I description BINDING SITE FOR RESIDUE ATP B 381 source : AC2 4) chain B residue 13 type sequence G description BINDING SITE FOR RESIDUE ATP B 381 source : AC2 5) chain B residue 14 type sequence T description BINDING SITE FOR RESIDUE ATP B 381 source : AC2 6) chain B residue 18 type sequence V description BINDING SITE FOR RESIDUE ATP B 381 source : AC2 7) chain B residue 31 type sequence A description BINDING SITE FOR RESIDUE ATP B 381 source : AC2 8) chain B residue 33 type sequence K description BINDING SITE FOR RESIDUE ATP B 381 source : AC2 9) chain B residue 81 type sequence E description BINDING SITE FOR RESIDUE ATP B 381 source : AC2 10) chain B residue 82 type sequence F description BINDING SITE FOR RESIDUE ATP B 381 source : AC2 11) chain B residue 83 type sequence L description BINDING SITE FOR RESIDUE ATP B 381 source : AC2 12) chain B residue 86 type sequence D description BINDING SITE FOR RESIDUE ATP B 381 source : AC2 13) chain B residue 89 type sequence K description BINDING SITE FOR RESIDUE ATP B 381 source : AC2 14) chain B residue 127 type sequence D description BINDING SITE FOR RESIDUE ATP B 381 source : AC2 15) chain B residue 129 type sequence K description BINDING SITE FOR RESIDUE ATP B 381 source : AC2 16) chain B residue 131 type sequence Q description BINDING SITE FOR RESIDUE ATP B 381 source : AC2 17) chain B residue 132 type sequence N description BINDING SITE FOR RESIDUE ATP B 381 source : AC2 18) chain B residue 145 type sequence D description BINDING SITE FOR RESIDUE ATP B 381 source : AC2 19) chain B residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 20) chain B residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 21) chain B residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 22) chain B residue 9 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 23) chain B residue 88 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 24) chain B residue 166 type SITE sequence L description CDK7 binding source Swiss-Prot : SWS_FT_FI4 25) chain B residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 26) chain B residue 14 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:17095507 source Swiss-Prot : SWS_FT_FI7 27) chain B residue 15 type MOD_RES sequence Y description Phosphotyrosine; by WEE1 => ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:17095507, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI8 28) chain B residue 19 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI9 29) chain B residue 160 type MOD_RES sequence X description Phosphothreonine; by CAK and CCRK => ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:14597612, ECO:0000269|PubMed:16325401, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:17570665, ECO:0000269|PubMed:20147522, ECO:0000269|PubMed:20360007, ECO:0000269|PubMed:21565702, ECO:0000305|PubMed:28666995 source Swiss-Prot : SWS_FT_FI10 30) chain B residue 10-33 type prosite sequence IGEGTYGVVYKARNKLTGEVVALK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGVVYkArnkltgev..........VALK source prosite : PS00107 31) chain B residue 123-135 type prosite sequence VLHRDLKPQNLLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpqNLLI source prosite : PS00108 32) chain B residue 33 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI2 33) chain B residue 81 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI2 34) chain B residue 86 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI2 35) chain B residue 129 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI2 36) chain B residue 10 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI2 37) chain B residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5

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