eF-site ID 5nvz-ABCDEFGHIJKL PDB Code 5nvz Chain A, B, C, D, E, F, G, H, I, J, K, L click to enlarge Title pVHL:EloB:EloC in complex with (2S,4R)-1-((S)-2-(1-acetylcyclopropanecarboxamido)-3,3-dimethylbutanoyl)-4-hydroxy-N-(4-(4-methylthiazol-5-yl)benzyl)pyrrolidine-2-carboxamide (ligand 16) Classification LIGASE Compound Elongin-B Source Homo sapiens (Human) (VHL_HUMAN) Sequence A:  MDVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPD EQRLYKDDQLLDDGKTLGEXGFTSQTARPQAPATVGLAFR ADDTFEALXIEPFSSPPELPDVMK B:  MMYVKLISSDGHEFIVKREHALTSGTIKAMLSNEVNFREI PSHVLSKVCMYFTYKVRYTNSSTEIPEFPIAPEIALELLM AANFLDC C:  VLRSVNSREPSQVIFXNRSPRVVLPVWLNFDGEPQPYPTL PPGTGRRIHSYRGHLWLFRDAGTHDGLLVNQTELFVPSLN VDGQPIFANITLPVYTLKERCLQVVRSLVKPENYRRLDIV RSLYEDLEDHPNVQKDLERLTQ D:  MDVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPD EQRLYKDDQLLDDGKTLGEXGFTSQTARPQAPATVGLAFR ADDTFEALXIEPFSSPPELPDVM E:  MMYVKLISSDGHEFIVKREHALTSGTIKAMLSGNETNEVN FREIPSHVLSKVCMYFTYKVRYTNSSTEIPEFPIAPEIAL ELLMAANFLDC F:  VLRSVNSREPSQVIFXNRSPRVVLPVWLNFDGEPQPYPTL PPGTGRRIHSYRGHLWLFRDAGTHDGLLVNQTELFVPSLN VDGQPIFANITLPVYTLKERCLQVVRSLVKPENYRRLDIV RSLYEDLEDHPNVQKDLERLTQE G:  MDVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPD EQRLYKDDQLLDDGKTLGEXGFTSQTARPQAPATVGLAFR ADDTFEALXIEPFSSPPELPDVM H:  MMYVKLISSDGHEFIVKREHALTSGTIKAMLSGTNEVNFR EIPSHVLSKVCMYFTYKVRYTNSSTEIPEFPIAPEIALEL LMAANFLDC I:  VLRSVNSREPSQVIFXNRSPRVVLPVWLNFDGEPQPYPTL PPGTGRRIHSYRGHLWLFRDAGTHDGLLVNQTELFVPSLN VDGQPIFANITLPVYTLKERCLQVVRSLVKPENYRRLDIV RSLYEDLEDHPNVQKDLERLTQE J:  MDVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPD EQRLYKDDQLLDDGKTLGEXGFTSQTARPQAPATVGLAFR ADDTFEALXIEPFSSPPELPDVM K:  MMYVKLISSDGHEFIVKREHALTSGTIKAMLSTNEVNFRE IPSHVLSKVCMYFTYKVRYTNSSTEIPEFPIAPEIALELL MAANFLDC L:  VLRSVNSREPSQVIFXNRSPRVVLPVWLNFDGEPQPYPTL PPGTGRRIHSYRGHLWLFRDAGTHDGLLVNQTELFVPSLN VDGQPIFANITLPVYTLKERCLQVVRSLVKPENYRRLDIV RSLYEDLEDHPNVQKDLERLTQE Description Functional site 1) chain C residue 88 type sequence W description binding site for residue 9BN C 301 source : AC1 2) chain C residue 98 type sequence Y description binding site for residue 9BN C 301 source : AC1 3) chain C residue 99 type sequence P description binding site for residue 9BN C 301 source : AC1 4) chain C residue 109 type sequence I description binding site for residue 9BN C 301 source : AC1 5) chain C residue 110 type sequence H description binding site for residue 9BN C 301 source : AC1 6) chain C residue 111 type sequence S description binding site for residue 9BN C 301 source : AC1 7) chain C residue 112 type sequence Y description binding site for residue 9BN C 301 source : AC1 8) chain C residue 115 type sequence H description binding site for residue 9BN C 301 source : AC1 9) chain C residue 117 type sequence W description binding site for residue 9BN C 301 source : AC1 10) chain L residue 182 type sequence R description binding site for residue 9BN C 301 source : AC1 11) chain F residue 67 type sequence N description binding site for residue 9BN F 301 source : AC2 12) chain F residue 69 type sequence R description binding site for residue 9BN F 301 source : AC2 13) chain F residue 88 type sequence W description binding site for residue 9BN F 301 source : AC2 14) chain F residue 98 type sequence Y description binding site for residue 9BN F 301 source : AC2 15) chain F residue 99 type sequence P description binding site for residue 9BN F 301 source : AC2 16) chain F residue 109 type sequence I description binding site for residue 9BN F 301 source : AC2 17) chain F residue 110 type sequence H description binding site for residue 9BN F 301 source : AC2 18) chain F residue 111 type sequence S description binding site for residue 9BN F 301 source : AC2 19) chain F residue 112 type sequence Y description binding site for residue 9BN F 301 source : AC2 20) chain F residue 115 type sequence H description binding site for residue 9BN F 301 source : AC2 21) chain F residue 117 type sequence W description binding site for residue 9BN F 301 source : AC2 22) chain I residue 182 type sequence R description binding site for residue 9BN F 301 source : AC2 23) chain I residue 67 type sequence N description binding site for residue 9BN I 301 source : AC3 24) chain I residue 88 type sequence W description binding site for residue 9BN I 301 source : AC3 25) chain I residue 91 type sequence F description binding site for residue 9BN I 301 source : AC3 26) chain I residue 98 type sequence Y description binding site for residue 9BN I 301 source : AC3 27) chain I residue 99 type sequence P description binding site for residue 9BN I 301 source : AC3 28) chain I residue 107 type sequence R description binding site for residue 9BN I 301 source : AC3 29) chain I residue 109 type sequence I description binding site for residue 9BN I 301 source : AC3 30) chain I residue 110 type sequence H description binding site for residue 9BN I 301 source : AC3 31) chain I residue 111 type sequence S description binding site for residue 9BN I 301 source : AC3 32) chain I residue 112 type sequence Y description binding site for residue 9BN I 301 source : AC3 33) chain I residue 115 type sequence H description binding site for residue 9BN I 301 source : AC3 34) chain I residue 117 type sequence W description binding site for residue 9BN I 301 source : AC3 35) chain C residue 182 type sequence R description binding site for residue 9BN L 301 source : AC4 36) chain L residue 67 type sequence N description binding site for residue 9BN L 301 source : AC4 37) chain L residue 88 type sequence W description binding site for residue 9BN L 301 source : AC4 38) chain L residue 98 type sequence Y description binding site for residue 9BN L 301 source : AC4 39) chain L residue 99 type sequence P description binding site for residue 9BN L 301 source : AC4 40) chain L residue 107 type sequence R description binding site for residue 9BN L 301 source : AC4 41) chain L residue 109 type sequence I description binding site for residue 9BN L 301 source : AC4 42) chain L residue 110 type sequence H description binding site for residue 9BN L 301 source : AC4 43) chain L residue 111 type sequence S description binding site for residue 9BN L 301 source : AC4 44) chain L residue 112 type sequence Y description binding site for residue 9BN L 301 source : AC4 45) chain L residue 115 type sequence H description binding site for residue 9BN L 301 source : AC4 46) chain L residue 117 type sequence W description binding site for residue 9BN L 301 source : AC4 47) chain A residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI1 48) chain D residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI1 49) chain G residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI1 50) chain J residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI1 51) chain A residue 84 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P62869 source Swiss-Prot : SWS_FT_FI2 52) chain D residue 84 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P62869 source Swiss-Prot : SWS_FT_FI2 53) chain G residue 84 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P62869 source Swiss-Prot : SWS_FT_FI2 54) chain J residue 84 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P62869 source Swiss-Prot : SWS_FT_FI2

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