eF-site ID 6h0f-ABCDEFGHIJKL PDB Code 6h0f Chain A, B, C, D, E, F, G, H, I, J, K, L Title Structure of DDB1-CRBN-pomalidomide complex bound to IKZF1(ZF2) Classification SIGNALING PROTEIN Compound DNA damage-binding protein 1,DNA damage-binding protein 1,DNA damage-binding protein 1,DNA damage-binding protein 1 Source (IKZF1_HUMAN) Sequence A:  MSYNYVVTAQKPTAVNGCVTGHFTSAEDLNLLIAKNTRLE IYVVTAEGLRPVKEVGMYGKIAVMELFRPKGESKDLLFIL TAKYNACILEYKQSGESIDIITRAHGNVQDRIGRPSETGI IGIIDPECRMIGLRLYDGLFKVIPLDRDNKELKAFNIRLE ELHVIDVKFLYGCQAPTICFVYQDPQGRHVKTYEVSLREK EFNKGPWKQENVEAEASMVIAVPEPFGGAIIIGQESITYH NGDKYLAIAPPIIKQSTIVCHNRVDPNGSRYLLGDMEGRL FMLLLEKEEQMDGTVTLKDLRVELLGETSIAECLTYLDNG VVFVGSRLGDSQLVKLNVDSNEQGSYVVAMETFTNLGPIV DMCVVDLERQGQGQLVTCSGAFKEGSLRIIRNGIKLHIRT VPLYESPRKICYQEVSQCFGVLSSRIEVQDTSGGTTALRP SASTQALSSSVSSSKLFSSSTAPHETSFGEEVEVHNLLII DQHTFEVLHAHQFLQNEYALSLVSCKLGKDPNTYFIVGTA MVYPEEAEPKQGRIVVFQYSDGKLQTVAEKEVKGAVYSMV EFNGKLLASINSTVRLYEWTTEKELRTECNHYNNIMALYL KTKGDFILVGDLMRSVLLLAYKPMEGNFEEIARDFNPNWM SAVEILDDDNFLGAENAFNLFVCQKDSAATTDEERQHLQE VGLFHLGEFVNVFCHGSLVMQNLGETSTPTQGSVLFGTVN GMIGLVTSLSESWYNLLLDMQNRLNKVIKSVGKIEHSFWR SFHTERKTEPATGFIDGDLIESFLDISRPKMQEVVANLQY DDGSGMKREATADDLIKVVEELTRIH B:  GRTLHDDDSCQVIPVLPQVMMILIPGQTLPLQLFHPQEVS MVRNLIQKDRTFAVLAYSNVQEREAQFGTTAEIYAYREEQ DFGIEIVKVKAIGRQRFKVLELRTQSDGIQQAKVQILPEC VLPSTMSAVQLESLNKCQIFPSKPVSREDQCSYKWWQKYQ KRKFHCANLTSWPRWLYSLYDAETLMDRIKKQLREWDENL KDDSLPSNPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRL RCELDIMNKCTSLCCKQCQETEITTKNEIFSLSLCGPMAA YVNPHGYVHETLTVYKACNLNLIGRPSTEHSWFPGYAWTV AQCKICASHIGWKFTATKKDMSPQKFWGLTRSALLPTIPD TEDEISPDKVILCL C:  GGRGERPFQCNQCGASFTQKGNLLRHIKLHSG D:  MSYNYVVTAQKPTAVNGCVTGHFTSAEDLNLLIAKNTRLE IYVVTAEGLRPVKEVGMYGKIAVMELFRPKGESKDLLFIL TAKYNACILEYKQSGESIDIITRAHGNVQDRIGRPSETGI IGIIDPECRMIGLRLYDGLFKVIPLDRDNKELKAFNIRLE ELHVIDVKFLYGCQAPTICFVYQDPQGRHVKTYEVSLREK EFNKGPWKQENVEAEASMVIAVPEPFGGAIIIGQESITYH NGDKYLAIAPPIIKQSTIVCHNRVDPNGSRYLLGDMEGRL FMLLLEKEEQMDGTVTLKDLRVELLGETSIAECLTYLDNG VVFVGSRLGDSQLVKLNVDSNEQGSYVVAMETFTNLGPIV DMCVVDLERQGQGQLVTCSGAFKEGSLRIIRNGIQKLHIR TVPLYESPRKICYQEVSQCFGVLSSRIEVQDTSGGTTALR PSASTQALSSSVSSSKLFSSSTAPHETSFGEEVEVHNLLI IDQHTFEVLHAHQFLQNEYALSLVSCKLGKDPNTYFIVGT AMVYPEEAEPKQGRIVVFQYSDGKLQTVAEKEVKGAVYSM VEFNGKLLASINSTVRLYEWTTEKELRTECNHYNNIMALY LKTKGDFILVGDLMRSVLLLAYKPMEGNFEEIARDFNPNW MSAVEILDDDNFLGAENAFNLFVCQKDSAATTDEERQHLQ EVGLFHLGEFVNVFCHGSLVMQTPTQGSVLFGTVNGMIGL VTSLSESWYNLLLDMQNRLNKVIKSVGKIEHSFWRSFHTE RKTEPATGFIDGDLIESFLDISRPKMQEVVANLQYDDGSG MKREATADDLIKVVEELTRIH E:  GRTLHDDDSCQVIPVLPQVMMILIPGQTLPLQLFHPQEVS MVRNLIQKDRTFAVLAYSNVQEREAQFGTTAEIYAYREEQ DFGIEIVKVKAIGRQRFKVLELRTQSDGIQQAKVQILPEC VLPSTMSAVQLESLNKCQIFPSKPVSREDQCSYKWWQKYQ KRKFHCANLTSWPRWLYSLYDAETLMDRIKKQLREWDENL KDDSLPSNPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRL RCELDIMNKCTSLCCKQCQETEITTKNEIFSLSLCGPMAA YVNPHGYVHETLTVYKACNLNLIGRPSTEHSWFPGYAWTV AQCKICASHIGWKFTATKKDMSPQKFWGLTRSALLPTIPD TEDEISPDKVILCL F:  GGRGERPFQCNQCGASFTQKGNLLRHIKLHSG G:  MSYNYVVTAQKPTAVNGCVTGHFTSAEDLNLLIAKNTRLE IYVVTAEGLRPVKEVGMYGKIAVMELFRPKGESKDLLFIL TAKYNACILEYKQSGESIDIITRAHGNVQDRIGRPSETGI IGIIDPECRMIGLRLYDGLFKVIPLDRDNKELKAFNIRLE ELHVIDVKFLYGCQAPTICFVYQDPQGRHVKTYEVSLREK EFNKGPWKQENVEAEASMVIAVPEPFGGAIIIGQESITYH NGDKYLAIAPPIIKQSTIVCHNRVDPNGSRYLLGDMEGRL FMLLLEKEEQMDGTVTLKDLRVELLGETSIAECLTYLDNG VVFVGSRLGDSQLVKLNVDSNEQGSYVVAMETFTNLGPIV DMCVVDLERQGQGQLVTCSGAFKEGSLRIIRNGIKLHIRT VPLYESPRKICYQEVSQCFGVLSSRIEVQDTSGGTTALRP SASTQALSSSVSSSKLFSSSTAPHETSFGEEVEVHNLLII DQHTFEVLHAHQFLQNEYALSLVSCKLGKDPNTYFIVGTA MVYPEEAEPKQGRIVVFQYSDGKLQTVAEKEVKGAVYSMV EFNGKLLASINSTVRLYEWTTEKELRTECNHYNNIMALYL KTKGDFILVGDLMRSVLLLAYKPMEGNFEEIARDFNPNWM SAVEILDDDNFLGAENAFNLFVCQKDSAATTDEERQHLQE VGLFHLGEFVNVFCHGSLVMQNLGETSTPTQGSVLFGTVN GMIGLVTSLSESWYNLLLDMQNRLNKVIKSVGKIEHSFWR SFHTERKTEPATGFIDGDLIESFLDISRPKMQEVVANLQY DDGSGMKREATADDLIKVVEELTRIH H:  GRTLHDDDSCQVIPVLPQVMMILIPGQTLPLQLFHPQEVS MVRNLIQKDRTFAVLAYSNVQEREAQFGTTAEIYAYREEQ DFGIEIVKVKAIGRQRFKVLELRTQSDGIQQAKVQILPEC VLPSTMSAVQLESLNKCQIFPSKPVSREDQCSYKWWQKYQ KRKFHCANLTSWPRWLYSLYDAETLMDRIKKQLREWDENL KDDSLPSNPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRL RCELDIMNKCTSLCCKQCQETEITTKNEIFSLSLCGPMAA YVNPHGYVHETLTVYKACNLNLIGRPSTEHSWFPGYAWTV AQCKICASHIGWKFTATKKDMSPQKFWGLTRSALLPTIPD TEDEISPDKVILCL I:  GGRGERPFQCNQCGASFTQKGNLLRHIKLHSG J:  EENLYFQGGGRMSYNYVVTAQKPTAVNGCVTGHFTSAEDL NLLIAKNTRLEIYVVTAEGLRPVKEVGMYGKIAVMELFRP KGESKDLLFILTAKYNACILEYKQSGESIDIITRAHGNVQ DRIGRPSETGIIGIIDPECRMIGLRLYDGLFKVIPLDRDN KELKAFNIRLEELHVIDVKFLYGCQAPTICFVYQDPQGRH VKTYEVSLREKEFNKGPWKQENVEAEASMVIAVPEPFGGA IIIGQESITYHNGDKYLAIAPPIIKQSTIVCHNRVDPNGS RYLLGDMEGRLFMLLLEKEEQMDGTVTLKDLRVELLGETS IAECLTYLDNGVVFVGSRLGDSQLVKLNVDSNEQGSYVVA METFTNLGPIVDMCVVDLERQGQGQLVTCSGAFKEGSLRI IRNGIGGGEIQKLHIRTVPLYESPRKICYQEVSQCFGVLS SRIEVQDTSGGTTALRPSASTQALSSSVSSSKLFSSSTAP HETSFGEEVEVHNLLIIDQHTFEVLHAHQFLQNEYALSLV SCKLGKDPNTYFIVGTAMVYPEEAEPKQGRIVVFQYSDGK LQTVAEKEVKGAVYSMVEFNGKLLASINSTVRLYEWTTEK ELRTECNHYNNIMALYLKTKGDFILVGDLMRSVLLLAYKP MEGNFEEIARDFNPNWMSAVEILDDDNFLGAENAFNLFVC QKDSAATTDEERQHLQEVGLFHLGEFVNVFCHGSLVMQNL GETSTPTQGSVLFGTVNGMIGLVTSLSESWYNLLLDMQNR LNKVIKSVGKIEHSFWRSFHTERKTEPATGFIDGDLIESF LDISRPKMQEVVANLQYDDGSGMKREATADDLIKVVEELT RIH K:  GRTLHDDDSCQVIPVLPQVMMILIPGQTLPLQLFHPQEVS MVRNLIQKDRTFAVLAYSNVQEREAQFGTTAEIYAYREEQ DFGIEIVKVKAIGRQRFKVLELRTQSDGIQQAKVQILPEC VLPSTMSAVQLESLNKCQIFPSKPVSREDQCSYKWWQKYQ KRKFHCANLTSWPRWLYSLYDAETLMDRIKKQLREWDENL KDDSLPSNPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRL RCELDIMNKCTSLCCKQCQETEITTKNEIFSLSLCGPMAA YVNPHGYVHETLTVYKACNLNLIGRPSTEHSWFPGYAWTV AQCKICASHIGWKFTATKKDMSPQKFWGLTRSALLPTIPD TEDEISPDKVILCL L:  GGRGERPFQCNQCGASFTQKGNLLRHIKLHSG Description Functional site 1) chain B residue 323 type sequence C description binding site for residue ZN B 501 source : AC1 2) chain B residue 326 type sequence C description binding site for residue ZN B 501 source : AC1 3) chain B residue 391 type sequence C description binding site for residue ZN B 501 source : AC1 4) chain B residue 394 type sequence C description binding site for residue ZN B 501 source : AC1 5) chain B residue 351 type sequence N description binding site for residue Y70 B 502 source : AC2 6) chain B residue 352 type sequence P description binding site for residue Y70 B 502 source : AC2 7) chain B residue 353 type sequence H description binding site for residue Y70 B 502 source : AC2 8) chain B residue 377 type sequence E description binding site for residue Y70 B 502 source : AC2 9) chain B residue 378 type sequence H description binding site for residue Y70 B 502 source : AC2 10) chain B residue 380 type sequence W description binding site for residue Y70 B 502 source : AC2 11) chain B residue 386 type sequence W description binding site for residue Y70 B 502 source : AC2 12) chain B residue 400 type sequence W description binding site for residue Y70 B 502 source : AC2 13) chain B residue 402 type sequence F description binding site for residue Y70 B 502 source : AC2 14) chain C residue 146 type sequence Q description binding site for residue Y70 B 502 source : AC2 15) chain C residue 147 type sequence C description binding site for residue Y70 B 502 source : AC2 16) chain C residue 148 type sequence N description binding site for residue Y70 B 502 source : AC2 17) chain C residue 149 type sequence Q description binding site for residue Y70 B 502 source : AC2 18) chain C residue 150 type sequence C description binding site for residue Y70 B 502 source : AC2 19) chain C residue 151 type sequence G description binding site for residue Y70 B 502 source : AC2 20) chain C residue 147 type sequence C description binding site for residue ZN C 201 source : AC3 21) chain C residue 150 type sequence C description binding site for residue ZN C 201 source : AC3 22) chain C residue 163 type sequence H description binding site for residue ZN C 201 source : AC3 23) chain C residue 167 type sequence H description binding site for residue ZN C 201 source : AC3 24) chain E residue 323 type sequence C description binding site for residue ZN E 501 source : AC4 25) chain E residue 326 type sequence C description binding site for residue ZN E 501 source : AC4 26) chain E residue 391 type sequence C description binding site for residue ZN E 501 source : AC4 27) chain E residue 394 type sequence C description binding site for residue ZN E 501 source : AC4 28) chain E residue 351 type sequence N description binding site for residue Y70 E 502 source : AC5 29) chain E residue 352 type sequence P description binding site for residue Y70 E 502 source : AC5 30) chain E residue 353 type sequence H description binding site for residue Y70 E 502 source : AC5 31) chain E residue 377 type sequence E description binding site for residue Y70 E 502 source : AC5 32) chain E residue 378 type sequence H description binding site for residue Y70 E 502 source : AC5 33) chain E residue 380 type sequence W description binding site for residue Y70 E 502 source : AC5 34) chain E residue 386 type sequence W description binding site for residue Y70 E 502 source : AC5 35) chain E residue 400 type sequence W description binding site for residue Y70 E 502 source : AC5 36) chain E residue 402 type sequence F description binding site for residue Y70 E 502 source : AC5 37) chain F residue 146 type sequence Q description binding site for residue Y70 E 502 source : AC5 38) chain F residue 147 type sequence C description binding site for residue Y70 E 502 source : AC5 39) chain F residue 148 type sequence N description binding site for residue Y70 E 502 source : AC5 40) chain F residue 149 type sequence Q description binding site for residue Y70 E 502 source : AC5 41) chain F residue 150 type sequence C description binding site for residue Y70 E 502 source : AC5 42) chain F residue 151 type sequence G description binding site for residue Y70 E 502 source : AC5 43) chain F residue 147 type sequence C description binding site for residue ZN F 201 source : AC6 44) chain F residue 150 type sequence C description binding site for residue ZN F 201 source : AC6 45) chain F residue 163 type sequence H description binding site for residue ZN F 201 source : AC6 46) chain F residue 167 type sequence H description binding site for residue ZN F 201 source : AC6 47) chain H residue 323 type sequence C description binding site for residue ZN H 501 source : AC7 48) chain H residue 326 type sequence C description binding site for residue ZN H 501 source : AC7 49) chain H residue 391 type sequence C description binding site for residue ZN H 501 source : AC7 50) chain H residue 394 type sequence C description binding site for residue ZN H 501 source : AC7 51) chain H residue 351 type sequence N description binding site for residue Y70 H 502 source : AC8 52) chain H residue 352 type sequence P description binding site for residue Y70 H 502 source : AC8 53) chain H residue 353 type sequence H description binding site for residue Y70 H 502 source : AC8 54) chain H residue 377 type sequence E description binding site for residue Y70 H 502 source : AC8 55) chain H residue 378 type sequence H description binding site for residue Y70 H 502 source : AC8 56) chain H residue 379 type sequence S description binding site for residue Y70 H 502 source : AC8 57) chain H residue 380 type sequence W description binding site for residue Y70 H 502 source : AC8 58) chain H residue 386 type sequence W description binding site for residue Y70 H 502 source : AC8 59) chain H residue 400 type sequence W description binding site for residue Y70 H 502 source : AC8 60) chain H residue 402 type sequence F description binding site for residue Y70 H 502 source : AC8 61) chain I residue 146 type sequence Q description binding site for residue Y70 H 502 source : AC8 62) chain I residue 147 type sequence C description binding site for residue Y70 H 502 source : AC8 63) chain I residue 148 type sequence N description binding site for residue Y70 H 502 source : AC8 64) chain I residue 149 type sequence Q description binding site for residue Y70 H 502 source : AC8 65) chain I residue 150 type sequence C description binding site for residue Y70 H 502 source : AC8 66) chain I residue 151 type sequence G description binding site for residue Y70 H 502 source : AC8 67) chain I residue 147 type sequence C description binding site for residue ZN I 201 source : AC9 68) chain I residue 150 type sequence C description binding site for residue ZN I 201 source : AC9 69) chain I residue 163 type sequence H description binding site for residue ZN I 201 source : AC9 70) chain I residue 167 type sequence H description binding site for residue ZN I 201 source : AC9 71) chain K residue 323 type sequence C description binding site for residue ZN K 501 source : AD1 72) chain K residue 326 type sequence C description binding site for residue ZN K 501 source : AD1 73) chain K residue 391 type sequence C description binding site for residue ZN K 501 source : AD1 74) chain K residue 394 type sequence C description binding site for residue ZN K 501 source : AD1 75) chain K residue 351 type sequence N description binding site for residue Y70 K 502 source : AD2 76) chain K residue 352 type sequence P description binding site for residue Y70 K 502 source : AD2 77) chain K residue 353 type sequence H description binding site for residue Y70 K 502 source : AD2 78) chain K residue 377 type sequence E description binding site for residue Y70 K 502 source : AD2 79) chain K residue 378 type sequence H description binding site for residue Y70 K 502 source : AD2 80) chain K residue 380 type sequence W description binding site for residue Y70 K 502 source : AD2 81) chain K residue 386 type sequence W description binding site for residue Y70 K 502 source : AD2 82) chain K residue 400 type sequence W description binding site for residue Y70 K 502 source : AD2 83) chain K residue 402 type sequence F description binding site for residue Y70 K 502 source : AD2 84) chain L residue 146 type sequence Q description binding site for residue Y70 K 502 source : AD2 85) chain L residue 147 type sequence C description binding site for residue Y70 K 502 source : AD2 86) chain L residue 148 type sequence N description binding site for residue Y70 K 502 source : AD2 87) chain L residue 149 type sequence Q description binding site for residue Y70 K 502 source : AD2 88) chain L residue 150 type sequence C description binding site for residue Y70 K 502 source : AD2 89) chain L residue 151 type sequence G description binding site for residue Y70 K 502 source : AD2 90) chain L residue 147 type sequence C description binding site for residue ZN L 201 source : AD3 91) chain L residue 150 type sequence C description binding site for residue ZN L 201 source : AD3 92) chain L residue 163 type sequence H description binding site for residue ZN L 201 source : AD3 93) chain L residue 167 type sequence H description binding site for residue ZN L 201 source : AD3 94) chain C residue 147-167 type prosite sequence CNQCGASFTQKGNLLRHIKLH description ZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. Cnq..CgasFtqkgnllrHikl..H source prosite : PS00028 95) chain A residue 2 type MOD_RES sequence S description N-acetylserine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI1 96) chain E residue 378 type MOD_RES sequence H description N-acetylserine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI1 97) chain E residue 380 type MOD_RES sequence W description N-acetylserine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI1 98) chain E residue 386 type MOD_RES sequence W description N-acetylserine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI1 99) chain E residue 391 type MOD_RES sequence C description N-acetylserine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI1 100) chain E residue 394 type MOD_RES sequence C description N-acetylserine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI1 101) chain H residue 323 type MOD_RES sequence C description N-acetylserine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI1 102) chain H residue 326 type MOD_RES sequence C description N-acetylserine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI1 103) chain H residue 378 type MOD_RES sequence H description N-acetylserine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI1 104) chain H residue 380 type MOD_RES sequence W description N-acetylserine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI1 105) chain H residue 386 type MOD_RES sequence W description N-acetylserine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI1 106) chain D residue 2 type MOD_RES sequence S description N-acetylserine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI1 107) chain H residue 391 type MOD_RES sequence C description N-acetylserine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI1 108) chain H residue 394 type MOD_RES sequence C description N-acetylserine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI1 109) chain K residue 323 type MOD_RES sequence C description N-acetylserine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI1 110) chain K residue 326 type MOD_RES sequence C description N-acetylserine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI1 111) chain K residue 378 type MOD_RES sequence H description N-acetylserine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI1 112) chain K residue 380 type MOD_RES sequence W description N-acetylserine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI1 113) chain K residue 386 type MOD_RES sequence W description N-acetylserine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI1 114) chain K residue 391 type MOD_RES sequence C description N-acetylserine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI1 115) chain K residue 394 type MOD_RES sequence C description N-acetylserine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI1 116) chain G residue 2 type MOD_RES sequence S description N-acetylserine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI1 117) chain J residue 2 type MOD_RES sequence S description N-acetylserine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI1 118) chain B residue 386 type MOD_RES sequence W description N-acetylserine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI1 119) chain B residue 391 type MOD_RES sequence C description N-acetylserine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI1 120) chain B residue 394 type MOD_RES sequence C description N-acetylserine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI1 121) chain E residue 323 type MOD_RES sequence C description N-acetylserine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI1 122) chain E residue 326 type MOD_RES sequence C description N-acetylserine => ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI1

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