eF-site ID 1ol1-ABCD PDB Code 1ol1 Chain A, B, C, D click to enlarge Title Cyclin A binding groove inhibitor H-Cit-Cit-Leu-Ile-(p-F-Phe)-NH2 Classification TRANSFERASE/TRANSFERASE INHIBITOR Compound CELL DIVISION PROTEIN KINASE 2 Source Homo sapiens (Human) (1OL1) 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:  VPDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAIL VDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQ LVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRM EHLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAM FLGELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSWPE SLIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYK NSKYHGVSLLNPPETLNL Description Functional site 1) chain A residue 12 type sequence E description BINDING SITE FOR CHAIN F OF CIR-CIR-LEU-ILE-PFF-NH2 source : AC1 2) chain A residue 13 type sequence G description BINDING SITE FOR CHAIN F OF CIR-CIR-LEU-ILE-PFF-NH2 source : AC1 3) chain A residue 163 type sequence V description BINDING SITE FOR CHAIN F OF CIR-CIR-LEU-ILE-PFF-NH2 source : AC1 4) chain A residue 165 type sequence T description BINDING SITE FOR CHAIN F OF CIR-CIR-LEU-ILE-PFF-NH2 source : AC1 5) chain B residue 210 type sequence M description BINDING SITE FOR CHAIN F OF CIR-CIR-LEU-ILE-PFF-NH2 source : AC1 6) chain B residue 214 type sequence L description BINDING SITE FOR CHAIN F OF CIR-CIR-LEU-ILE-PFF-NH2 source : AC1 7) chain B residue 217 type sequence W description BINDING SITE FOR CHAIN F OF CIR-CIR-LEU-ILE-PFF-NH2 source : AC1 8) chain B residue 250 type sequence R description BINDING SITE FOR CHAIN F OF CIR-CIR-LEU-ILE-PFF-NH2 source : AC1 9) chain B residue 254 type sequence Q description BINDING SITE FOR CHAIN F OF CIR-CIR-LEU-ILE-PFF-NH2 source : AC1 10) chain B residue 271 type sequence Y description BINDING SITE FOR CHAIN F OF CIR-CIR-LEU-ILE-PFF-NH2 source : AC1 11) chain B residue 281 type sequence I description BINDING SITE FOR CHAIN F OF CIR-CIR-LEU-ILE-PFF-NH2 source : AC1 12) chain B residue 283 type sequence D description BINDING SITE FOR CHAIN F OF CIR-CIR-LEU-ILE-PFF-NH2 source : AC1 13) chain B residue 285 type sequence T description BINDING SITE FOR CHAIN F OF CIR-CIR-LEU-ILE-PFF-NH2 source : AC1 14) chain C residue 247 type sequence D description BINDING SITE FOR CHAIN H OF CIR-CIR-LEU-ILE-PFF-NH2 source : AC2 15) chain D residue 210 type sequence M description BINDING SITE FOR CHAIN H OF CIR-CIR-LEU-ILE-PFF-NH2 source : AC2 16) chain D residue 214 type sequence L description BINDING SITE FOR CHAIN H OF CIR-CIR-LEU-ILE-PFF-NH2 source : AC2 17) chain D residue 217 type sequence W description BINDING SITE FOR CHAIN H OF CIR-CIR-LEU-ILE-PFF-NH2 source : AC2 18) chain D residue 250 type sequence R description BINDING SITE FOR CHAIN H OF CIR-CIR-LEU-ILE-PFF-NH2 source : AC2 19) chain D residue 254 type sequence Q description BINDING SITE FOR CHAIN H OF CIR-CIR-LEU-ILE-PFF-NH2 source : AC2 20) chain D residue 281 type sequence I description BINDING SITE FOR CHAIN H OF CIR-CIR-LEU-ILE-PFF-NH2 source : AC2 21) chain D residue 282 type sequence T description BINDING SITE FOR CHAIN H OF CIR-CIR-LEU-ILE-PFF-NH2 source : AC2 22) chain D residue 283 type sequence D description BINDING SITE FOR CHAIN H OF CIR-CIR-LEU-ILE-PFF-NH2 source : AC2 23) chain D residue 285 type sequence T description BINDING SITE FOR CHAIN H OF CIR-CIR-LEU-ILE-PFF-NH2 source : AC2 24) chain A residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 25) chain C residue 127 type ACT_SITE sequence D description Proton acceptor source Swiss-Prot : SWS_FT_FI1 26) 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 27) 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 28) 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 29) 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 30) 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 31) 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 32) 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 33) 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 34) 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 35) 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 36) 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 37) 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 38) chain A residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 39) chain A residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 40) chain C residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 41) chain C residue 145 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21565702 source Swiss-Prot : SWS_FT_FI3 42) chain A residue 9 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 43) chain A residue 88 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 44) chain A residue 166 type SITE sequence L description CDK7 binding source Swiss-Prot : SWS_FT_FI4 45) chain C residue 9 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 46) chain C residue 88 type SITE sequence K description CDK7 binding source Swiss-Prot : SWS_FT_FI4 47) chain C residue 166 type SITE sequence L description CDK7 binding source Swiss-Prot : SWS_FT_FI4 48) chain A residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 49) chain C residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI5 50) chain A residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 51) chain C residue 6 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 52) 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 53) 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 54) 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 55) 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 56) chain A residue 19 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI9 57) chain C residue 19 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI9 58) chain B residue 211-242 type prosite sequence RAILVDWLVEVGEEYKLQNETLHLAVNYIDRF description CYCLINS Cyclins signature. RaiLvdWLvevgeeykLqnetLhlAVnYIDRF source prosite : PS00292 59) chain A residue 10-33 type prosite sequence IGEGTYGVVYKARNKLTGEVVALK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGVVYkArnkltgev..........VALK source prosite : PS00107 60) chain A residue 123-135 type prosite sequence VLHRDLKPQNLLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpqNLLI source prosite : PS00108

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