eF-site ID 1okv-ABCDEF PDB Code 1okv Chain A, B, C, D, E, F click to enlarge Title Cyclin A binding groove inhibitor H-Arg-Arg-Leu-Ile-Phe-NH2 Classification TRANSFERASE/TRANSFERASE INHIBITOR Compound CELL DIVISION PROTEIN KINASE 2 Source null (1OKV) Sequence A:  MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTE TEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVF EFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYT HEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRR ALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAA LAHPFFQDVTKPVPHL B:  VPDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAIL VDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQ LVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRM EHLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAM FLGELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSWPE SLIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYK NSKYHGVSLLNPPETLNL C:  MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTE TEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVF EFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYT HEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRR ALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAA LAHPFFQDVTKPVPHL D:  NEVPDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRA ILVDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGK LQLVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVL RMEHLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESL AMFLGELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSW PESLIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREK YKNSKYHGVSLLNPPETLNL E:  RRLIFX F:  RRLIFX Description Functional site 1) chain A residue 13 type sequence G description BINDING SITE FOR CHAIN E OF H-ARG-ARG-LEU-ILE-PHE-NH2 source : AC1 2) chain A residue 163 type sequence V description BINDING SITE FOR CHAIN E OF H-ARG-ARG-LEU-ILE-PHE-NH2 source : AC1 3) chain B residue 210 type sequence M description BINDING SITE FOR CHAIN E OF H-ARG-ARG-LEU-ILE-PHE-NH2 source : AC1 4) chain B residue 217 type sequence W description BINDING SITE FOR CHAIN E OF H-ARG-ARG-LEU-ILE-PHE-NH2 source : AC1 5) chain B residue 220 type sequence E description BINDING SITE FOR CHAIN E OF H-ARG-ARG-LEU-ILE-PHE-NH2 source : AC1 6) chain B residue 250 type sequence R description BINDING SITE FOR CHAIN E OF H-ARG-ARG-LEU-ILE-PHE-NH2 source : AC1 7) chain B residue 253 type sequence L description BINDING SITE FOR CHAIN E OF H-ARG-ARG-LEU-ILE-PHE-NH2 source : AC1 8) chain B residue 254 type sequence Q description BINDING SITE FOR CHAIN E OF H-ARG-ARG-LEU-ILE-PHE-NH2 source : AC1 9) chain B residue 281 type sequence I description BINDING SITE FOR CHAIN E OF H-ARG-ARG-LEU-ILE-PHE-NH2 source : AC1 10) chain B residue 282 type sequence T description BINDING SITE FOR CHAIN E OF H-ARG-ARG-LEU-ILE-PHE-NH2 source : AC1 11) chain B residue 283 type sequence D description BINDING SITE FOR CHAIN E OF H-ARG-ARG-LEU-ILE-PHE-NH2 source : AC1 12) chain B residue 285 type sequence T description BINDING SITE FOR CHAIN E OF H-ARG-ARG-LEU-ILE-PHE-NH2 source : AC1 13) chain C residue 247 type sequence D description BINDING SITE FOR CHAIN F OF H-ARG-ARG-LEU-ILE-PHE-NH2 source : AC2 14) chain D residue 210 type sequence M description BINDING SITE FOR CHAIN F OF H-ARG-ARG-LEU-ILE-PHE-NH2 source : AC2 15) chain D residue 217 type sequence W description BINDING SITE FOR CHAIN F OF H-ARG-ARG-LEU-ILE-PHE-NH2 source : AC2 16) chain D residue 220 type sequence E description BINDING SITE FOR CHAIN F OF H-ARG-ARG-LEU-ILE-PHE-NH2 source : AC2 17) chain D residue 250 type sequence R description BINDING SITE FOR CHAIN F OF H-ARG-ARG-LEU-ILE-PHE-NH2 source : AC2 18) chain D residue 254 type sequence Q description BINDING SITE FOR CHAIN F OF H-ARG-ARG-LEU-ILE-PHE-NH2 source : AC2 19) chain D residue 281 type sequence I description BINDING SITE FOR CHAIN F OF H-ARG-ARG-LEU-ILE-PHE-NH2 source : AC2 20) chain D residue 283 type sequence D description BINDING SITE FOR CHAIN F OF H-ARG-ARG-LEU-ILE-PHE-NH2 source : AC2 21) chain D residue 285 type sequence T description BINDING SITE FOR CHAIN F OF H-ARG-ARG-LEU-ILE-PHE-NH2 source : AC2 22) chain A residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 23) chain C residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 24) chain C residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 27) chain C residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 28) chain C residue 9 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 29) chain C residue 88 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 30) chain C residue 166 type SITE sequence L description CDK7 binding source Swiss-Prot : SWS_FT_FI4 31) chain A residue 9 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 32) chain A residue 88 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 33) chain A residue 166 type SITE sequence L description CDK7 binding source Swiss-Prot : SWS_FT_FI4 34) chain C residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 35) chain A residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 36) chain A residue 14 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:17095507 source Swiss-Prot : SWS_FT_FI7 37) chain C residue 14 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:17095507 source Swiss-Prot : SWS_FT_FI7 38) chain A 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 39) chain C 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 40) chain A residue 19 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI9 41) chain C residue 19 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI9 42) chain A residue 160 type MOD_RES sequence T 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 43) chain C residue 160 type MOD_RES sequence T 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 44) chain A residue 10-33 type prosite sequence IGEGTYGVVYKARNKLTGEVVALK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGVVYkArnkltgev..........VALK source prosite : PS00107 45) chain A residue 123-135 type prosite sequence VLHRDLKPQNLLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpqNLLI source prosite : PS00108 46) chain B residue 211-242 type prosite sequence RAILVDWLVEVGEEYKLQNETLHLAVNYIDRF description CYCLINS Cyclins signature. RaiLvdWLvevgeeykLqnetLhlAVnYIDRF source prosite : PS00292 47) chain C 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 48) chain A 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 49) chain A 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 50) chain A 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 51) chain C 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 52) chain C 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 53) chain C 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 54) chain C 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 55) chain A 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 56) chain A 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 57) chain A residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 58) chain C residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5

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