eF-site ID 3zni-ABCDEFGHIJKLMNOP PDB Code 3zni Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P click to enlarge Title Structure of phosphoTyr363-Cbl-b - UbcH5B-Ub - ZAP-70 peptide complex Classification LIGASE Compound E3 UBIQUITIN-PROTEIN LIGASE CBL-B Source (UBC_HUMAN) Sequence A:  QAAADRRTVEKTWKLMDKVVRLCQNPKLQLKNSPPYILDI LPDTYQHLRLILSKYDDNQKLAQLSENEYFKIYIDSLMKK SKRAIRLFKEGKERMYEEQSQDRRNLTKLSLIFSHMLAEI KAIFPNGQFQGDNFRITKADAAEFWRKFFGDKTIVPWKVF RQCLHEVHQISSGLEAMALKSTIDLTCNDYISVFEFDIFT RLFQPWGSILRNWNFLAVTHPGYMAFLTYDEVKARLQKYS TKPGSYIFRLSCTRLGQWAIGYVTGDGNILQTIPHNKPLF QALIDGSREGFYLYPDGRSYNPDLTGLCEPTPHDHIKVTQ EQFELXCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCL TAWQESDGQGCPFCRCEIKGTEPIIVDPFD B:  SDGXTPEPA C:  ALKRIHKELNDLARDPPAQCRAGPVGDDMFHWQATIMGPN DSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNINSN GSIKLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVP EIARIYKTDREKYNRIAREWTQKYAM D:  SMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPD QQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG E:  QAAADRRTVEKTWKLMDKVVRLCQNPKLQLKNSPPYILDI LPDTYQHLRLILSKYDDNQKLAQLSENEYFKIYIDSLMKK SKRAIRLFKEGKERMYEEQSQDRRNLTKLSLIFSHMLAEI KAIFPNGQFQGDNFRITKADAAEFWRKFFGDKTIVPWKVF RQCLHEVHQISSGLEAMALKSTIDLTCNDYISVFEFDIFT RLFQPWGSILRNWNFLAVTHPGYMAFLTYDEVKARLQKYS TKPGSYIFRLSCTRLGQWAIGYVTGDGNILQTIPHNKPLF QALIDGSREGFYLYPDGRSYNPDLTGLCEPTPHDHIKVTQ EQFELXCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCL TAWQESDGQGCPFCRCEIKGTEPIIVDPFD F:  DGXTPEPA G:  ALKRIHKELNDLARDPPAQCRAGPVGDDMFHWQATIMGPN DSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNINSN GSIKLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVP EIARIYKTDREKYNRIAREWTQKYAM H:  SMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPD QQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG I:  ADRRTVEKTWKLMDKVVRLCQNPKLQLKNSPPYILDILPD TYQHLRLILSKYDDNQKLAQLSENEYFKIYIDSLMKKSKR AIRLFKEGKERMYEEQSQDRRNLTKLSLIFSHMLAEIKAI FPNGQFQGDNFRITKADAAEFWRKFFGDKTIVPWKVFRQC LHEVHQISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLF QPWGSILRNWNFLAVTHPGYMAFLTYDEVKARLQKYSTKP GSYIFRLSCTRLGQWAIGYVTGDGNILQTIPHNKPLFQAL IDGSREGFYLYPDGRSYNPDLTGLCEPTPHDHIKVTQEQF ELXCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTAW QESDGQGCPFCRCEIKGTEPIIVDPF J:  DGXTPEPA K:  ALKRIHKELNDLARDPPAQCRAGPVGDDMFHWQATIMGPN DSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNINSN GSIKLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVP EIARIYKTDREKYNRIAREWTQKYAM L:  SMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPD QQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG M:  QAAADRRTVEKTWKLMDKVVRLCQNPKLQLKNSPPYILDI LPDTYQHLRLILSKYDDNQKLAQLSENEYFKIYIDSLMKK SKRAIRLFKEGKERMYEEQSQDRRNLTKLSLIFSHMLAEI KAIFPNGQFQGDNFRITKADAAEFWRKFFGDKTIVPWKVF RQCLHEVHQISSGLEAMALKSTIDLTCNDYISVFEFDIFT RLFQPWGSILRNWNFLAVTHPGYMAFLTYDEVKARLQKYS TKPGSYIFRLSCTRLGQWAIGYVTGDGNILQTIPHNKPLF QALIDGSREGFYLYPDGRSYNPDLTGLCEPTPHDHIKVTQ EQFELXCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCL TAWQESDGQGCPFCRCEIKGTEPIIVDPFD N:  SDGXTPEPA O:  ALKRIHKELNDLARDPPAQCRAGPVGDDMFHWQATIMGPN DSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNINSN GSIKLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVP EIARIYKTDREKYNRIAREWTQKYAM P:  SMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPD QQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG Description Functional site 1) chain A residue 373 type sequence C description BINDING SITE FOR RESIDUE ZN A 1428 source : AC1 2) chain A residue 376 type sequence C description BINDING SITE FOR RESIDUE ZN A 1428 source : AC1 3) chain A residue 393 type sequence C description BINDING SITE FOR RESIDUE ZN A 1428 source : AC1 4) chain A residue 396 type sequence C description BINDING SITE FOR RESIDUE ZN A 1428 source : AC1 5) chain A residue 388 type sequence C description BINDING SITE FOR RESIDUE ZN A 1429 source : AC2 6) chain A residue 390 type sequence H description BINDING SITE FOR RESIDUE ZN A 1429 source : AC2 7) chain A residue 408 type sequence C description BINDING SITE FOR RESIDUE ZN A 1429 source : AC2 8) chain A residue 411 type sequence C description BINDING SITE FOR RESIDUE ZN A 1429 source : AC2 9) chain E residue 373 type sequence C description BINDING SITE FOR RESIDUE ZN E 1428 source : AC3 10) chain E residue 376 type sequence C description BINDING SITE FOR RESIDUE ZN E 1428 source : AC3 11) chain E residue 393 type sequence C description BINDING SITE FOR RESIDUE ZN E 1428 source : AC3 12) chain E residue 396 type sequence C description BINDING SITE FOR RESIDUE ZN E 1428 source : AC3 13) chain E residue 388 type sequence C description BINDING SITE FOR RESIDUE ZN E 1429 source : AC4 14) chain E residue 390 type sequence H description BINDING SITE FOR RESIDUE ZN E 1429 source : AC4 15) chain E residue 408 type sequence C description BINDING SITE FOR RESIDUE ZN E 1429 source : AC4 16) chain E residue 411 type sequence C description BINDING SITE FOR RESIDUE ZN E 1429 source : AC4 17) chain I residue 373 type sequence C description BINDING SITE FOR RESIDUE ZN I 1427 source : AC5 18) chain I residue 376 type sequence C description BINDING SITE FOR RESIDUE ZN I 1427 source : AC5 19) chain I residue 393 type sequence C description BINDING SITE FOR RESIDUE ZN I 1427 source : AC5 20) chain I residue 396 type sequence C description BINDING SITE FOR RESIDUE ZN I 1427 source : AC5 21) chain I residue 388 type sequence C description BINDING SITE FOR RESIDUE ZN I 1428 source : AC6 22) chain I residue 390 type sequence H description BINDING SITE FOR RESIDUE ZN I 1428 source : AC6 23) chain I residue 408 type sequence C description BINDING SITE FOR RESIDUE ZN I 1428 source : AC6 24) chain I residue 411 type sequence C description BINDING SITE FOR RESIDUE ZN I 1428 source : AC6 25) chain M residue 373 type sequence C description BINDING SITE FOR RESIDUE ZN M 1428 source : AC7 26) chain M residue 376 type sequence C description BINDING SITE FOR RESIDUE ZN M 1428 source : AC7 27) chain M residue 393 type sequence C description BINDING SITE FOR RESIDUE ZN M 1428 source : AC7 28) chain M residue 396 type sequence C description BINDING SITE FOR RESIDUE ZN M 1428 source : AC7 29) chain M residue 388 type sequence C description BINDING SITE FOR RESIDUE ZN M 1429 source : AC8 30) chain M residue 390 type sequence H description BINDING SITE FOR RESIDUE ZN M 1429 source : AC8 31) chain M residue 408 type sequence C description BINDING SITE FOR RESIDUE ZN M 1429 source : AC8 32) chain M residue 411 type sequence C description BINDING SITE FOR RESIDUE ZN M 1429 source : AC8 33) chain A residue 221 type sequence D description BINDING SITE FOR RESIDUE CA A 1430 source : AC9 34) chain A residue 223 type sequence T description BINDING SITE FOR RESIDUE CA A 1430 source : AC9 35) chain A residue 225 type sequence N description BINDING SITE FOR RESIDUE CA A 1430 source : AC9 36) chain A residue 227 type sequence Y description BINDING SITE FOR RESIDUE CA A 1430 source : AC9 37) chain A residue 232 type sequence E description BINDING SITE FOR RESIDUE CA A 1430 source : AC9 38) chain E residue 221 type sequence D description BINDING SITE FOR RESIDUE CA E 1430 source : BC1 39) chain E residue 223 type sequence T description BINDING SITE FOR RESIDUE CA E 1430 source : BC1 40) chain E residue 225 type sequence N description BINDING SITE FOR RESIDUE CA E 1430 source : BC1 41) chain E residue 227 type sequence Y description BINDING SITE FOR RESIDUE CA E 1430 source : BC1 42) chain E residue 232 type sequence E description BINDING SITE FOR RESIDUE CA E 1430 source : BC1 43) chain I residue 221 type sequence D description BINDING SITE FOR RESIDUE CA I 1429 source : BC2 44) chain I residue 223 type sequence T description BINDING SITE FOR RESIDUE CA I 1429 source : BC2 45) chain I residue 225 type sequence N description BINDING SITE FOR RESIDUE CA I 1429 source : BC2 46) chain I residue 227 type sequence Y description BINDING SITE FOR RESIDUE CA I 1429 source : BC2 47) chain I residue 232 type sequence E description BINDING SITE FOR RESIDUE CA I 1429 source : BC2 48) chain M residue 221 type sequence D description BINDING SITE FOR RESIDUE CA M 1430 source : BC3 49) chain M residue 223 type sequence T description BINDING SITE FOR RESIDUE CA M 1430 source : BC3 50) chain M residue 225 type sequence N description BINDING SITE FOR RESIDUE CA M 1430 source : BC3 51) chain M residue 227 type sequence Y description BINDING SITE FOR RESIDUE CA M 1430 source : BC3 52) chain M residue 232 type sequence E description BINDING SITE FOR RESIDUE CA M 1430 source : BC3 53) chain E residue 231 type sequence F description BINDING SITE FOR RESIDUE EDO E 1431 source : BC4 54) chain E residue 234 type sequence D description BINDING SITE FOR RESIDUE EDO E 1431 source : BC4 55) chain E residue 238 type sequence R description BINDING SITE FOR RESIDUE EDO E 1431 source : BC4 56) chain E residue 292 type sequence L description BINDING SITE FOR RESIDUE EDO E 1431 source : BC4 57) chain E residue 414 type sequence E description BINDING SITE FOR RESIDUE EDO E 1431 source : BC4 58) chain A residue 231 type sequence F description BINDING SITE FOR RESIDUE EDO A 1431 source : BC5 59) chain A residue 234 type sequence D description BINDING SITE FOR RESIDUE EDO A 1431 source : BC5 60) chain A residue 238 type sequence R description BINDING SITE FOR RESIDUE EDO A 1431 source : BC5 61) chain A residue 292 type sequence L description BINDING SITE FOR RESIDUE EDO A 1431 source : BC5 62) chain I residue 231 type sequence F description BINDING SITE FOR RESIDUE EDO I 1430 source : BC6 63) chain I residue 234 type sequence D description BINDING SITE FOR RESIDUE EDO I 1430 source : BC6 64) chain I residue 238 type sequence R description BINDING SITE FOR RESIDUE EDO I 1430 source : BC6 65) chain I residue 292 type sequence L description BINDING SITE FOR RESIDUE EDO I 1430 source : BC6 66) chain M residue 231 type sequence F description BINDING SITE FOR RESIDUE EDO M 1431 source : BC7 67) chain M residue 234 type sequence D description BINDING SITE FOR RESIDUE EDO M 1431 source : BC7 68) chain M residue 238 type sequence R description BINDING SITE FOR RESIDUE EDO M 1431 source : BC7 69) chain M residue 292 type sequence L description BINDING SITE FOR RESIDUE EDO M 1431 source : BC7 70) chain C residue 85 type ACT_SITE sequence K description Glycyl thioester intermediate => ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133 source Swiss-Prot : SWS_FT_FI1 71) chain G residue 85 type ACT_SITE sequence K description Glycyl thioester intermediate => ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133 source Swiss-Prot : SWS_FT_FI1 72) chain K residue 85 type ACT_SITE sequence K description Glycyl thioester intermediate => ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133 source Swiss-Prot : SWS_FT_FI1 73) chain O residue 85 type ACT_SITE sequence K description Glycyl thioester intermediate => ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133 source Swiss-Prot : SWS_FT_FI1 74) chain B residue 7 type MOD_RES sequence X description Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI2 75) chain F residue 7 type MOD_RES sequence X description Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI2 76) chain J residue 7 type MOD_RES sequence X description Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI2 77) chain N residue 7 type MOD_RES sequence X description Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI2 78) chain E residue 232 type MOD_RES sequence E description Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI2 79) chain I residue 221 type MOD_RES sequence D description Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI2 80) chain I residue 223 type MOD_RES sequence T description Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI2 81) chain I residue 225 type MOD_RES sequence N description Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI2 82) chain I residue 227 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI2 83) chain I residue 232 type MOD_RES sequence E description Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI2 84) chain M residue 221 type MOD_RES sequence D description Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI2 85) chain M residue 223 type MOD_RES sequence T description Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI2 86) chain M residue 225 type MOD_RES sequence N description Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI2 87) chain M residue 227 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI2 88) chain M residue 232 type MOD_RES sequence E description Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI2 89) chain A residue 232 type MOD_RES sequence E description Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI2 90) chain E residue 221 type MOD_RES sequence D description Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI2 91) chain E residue 223 type MOD_RES sequence T description Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI2 92) chain E residue 225 type MOD_RES sequence N description Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI2 93) chain E residue 227 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI2 94) chain A residue 286 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 95) chain E residue 286 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 96) chain I residue 286 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 97) chain M residue 286 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 98) chain A residue 282 type MOD_RES sequence S description Phosphoserine; by PKC/PRKCQ => ECO:0000269|PubMed:19549985 source Swiss-Prot : SWS_FT_FI4 99) chain E residue 282 type MOD_RES sequence S description Phosphoserine; by PKC/PRKCQ => ECO:0000269|PubMed:19549985 source Swiss-Prot : SWS_FT_FI4 100) chain I residue 282 type MOD_RES sequence S description Phosphoserine; by PKC/PRKCQ => ECO:0000269|PubMed:19549985 source Swiss-Prot : SWS_FT_FI4 101) chain M residue 282 type MOD_RES sequence S description Phosphoserine; by PKC/PRKCQ => ECO:0000269|PubMed:19549985 source Swiss-Prot : SWS_FT_FI4 102) chain A residue 363 type MOD_RES sequence X description Phosphotyrosine => ECO:0000305|PubMed:20525694 source Swiss-Prot : SWS_FT_FI5 103) chain E residue 363 type MOD_RES sequence X description Phosphotyrosine => ECO:0000305|PubMed:20525694 source Swiss-Prot : SWS_FT_FI5 104) chain I residue 363 type MOD_RES sequence X description Phosphotyrosine => ECO:0000305|PubMed:20525694 source Swiss-Prot : SWS_FT_FI5 105) chain M residue 363 type MOD_RES sequence X description Phosphotyrosine => ECO:0000305|PubMed:20525694 source Swiss-Prot : SWS_FT_FI5 106) chain D residue 27-52 type prosite sequence KAKIQDKEGIPPDQQRLIFAGKQLED description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD source prosite : PS00299 107) chain A residue 388-397 type prosite sequence CGHLMCTSCL description ZF_RING_1 Zinc finger RING-type signature. CgHlMCtsCL source prosite : PS00518

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