eF-site ID 6h3c-ABCDEFGHIJ PDB Code 6h3c Chain A, B, C, D, E, F, G, H, I, J click to enlarge Title Cryo-EM structure of the BRISC complex bound to SHMT2 Classification SIGNALING PROTEIN Compound BRISC complex subunit Abraxas 2 Source (GLYM_HUMAN) Sequence A:  MAASISGYTFSAVCFHSANSNADHEGFLLGEVRQEETFSI SDSQISNTEFLQVIEIHNHQPCSKLFSFYDYASKVNEESL DRILKDRRKKVIGWYRFRRNTQQQMSYREQVLHKQLTRIL GVPDLVFLLFSFISTANNSTHALEYVLFRPNRRYNQRISL AIPNLGNTSQQEYKVSSVPNTSQSYAKVIKEHGTDFFDKD GVMKDIRAIYQVYNALQEKVQAVCADVEKSERVVESCQAE VNKLRRQITQRKNEK B:  AVQAVHLESDAFLVCLNHALSTEKEEVMGLCIGELNDDTV RIVHIHSVIILRRSDKRKDRVEISPEQLSAASTEAERLAE LTGRPMRVVGWYHSHPHITVWPSHVDVRTQAMYQMMDQGF VGLIFSCFIEDKNTKTGRVLYTCFQSIQAQYERIEIPIHI VPHVTIGKVCLESAVELPKILCQEEQDAYRRIHSLTHLDS VTKIHNGSVFTKNLCSQMSAVSGPLLQWLEDRLEQNQQHL QELQQEKEELMQELSSLE C:  MSPEVALNRISPMLSPFISSVVRNGKVGLDATNCLRITDL KSGCTSLTPGPNCDRFKLHIPYAGETLKWDIIFNAQYPEL PPDFIFGEDAEFLPDPSALQNLASWNPSNPECLLLVVKEL VQQYHQFQCSRLRESSRLMFEYQTLLEEPQYGENMEIYAG KKNNWTGEFSARFLLKLPVDFSNIPTYLLKDVNEDPGEDV ALLSVSFEDTEATQVYPKLYLSPRIEHALGGSSALHIPAF PGGGCLIDYVPQVCHLLTNKVQYVIQGYHKRREYIAAFLS HFGTGVVEYDAEGFTKLTLLLMWKDFCFLVHIDLPLFFPR DQPTLTFQSVYHFTNSGQLYSQAQKNYPYSPRWDGNEMAK RAKAYFKTFVPQFQEAAFANGKL D:  EVQIRTPRVNCPEKVIICLDLSEEMSLPKLESFNGSKTNA LNVSQKMIEMFVRTKHKIDKSHEFALVVVNDDTAWLSGLT SDPRELCSCLYDLETASCSTFNLEGLFSLIQQKTELPVTE NVQTIPPPYVVRTILVYSRPPCQPQFSLTEPMKKMFQCPY FFFDVVYIHNGTEEKEEEMSWKDMFAFMGSLDTKGTSYKY EVALAGPALELHNCMAKLLAHPLQRPCQSHASYSLLE E:  WTGQESLSDSDPEMWELLQREKDRQCRGLELIASENFCSR AALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRR ALEAFDLDPAQWGVNVQPYSGSPANLAVYTALLQPHDRIM GLDLSIFFESMPYKLNPKTGLIDYNQLALTARLFRPRLII AGTSAYARLIDYARMREVCDEVKAHLLADMAHISGLVAAK VIPSPFKHADIVTTTTHKTLRGTRSGLIFYRKGVKAVDPK TGREIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQA CTPMFREYSLQVLKNARAMADALLERGYSLVSGGTDNHLV LVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPG GLRLGAPALTSRQFREDDFRRVVDFIDEGVNIGLEVKSKT AKLQDFKSFLLKDSETSQRLANLRQRVEQFARAFPMPGFD F:  MAASISGYTFSAVCFHSANSNADHEGFLLGEVRQEETFSI SDSQISNTEFLQVIEIHNHQPCSKLFSFYDYASKVNEESL DRILKDRRKKVIGWYRFRRNTQQQMSYREQVLHKQLTRIL GVPDLVFLLFSFISTANNSTHALEYVLFRPNRRYNQRISL AIPNLGNTSQQEYKVSSVPNTSQSYAKVIKEHGTDFFDKD GVMKDIRAIYQVYNALQEKVQAVCADVEKSERVVESCQAE VNKLRRQITQRKNEK G:  AVQAVHLESDAFLVCLNHALSTEKEEVMGLCIGELNDDTV RIVHIHSVIILRRSDKRKDRVEISPEQLSAASTEAERLAE LTGRPMRVVGWYHSHPHITVWPSHVDVRTQAMYQMMDQGF VGLIFSCFIEDKNTKTGRVLYTCFQSIQAQYERIEIPIHI VPHVTIGKVCLESAVELPKILCQEEQDAYRRIHSLTHLDS VTKIHNGSVFTKNLCSQMSAVSGPLLQWLEDRLEQNQQHL QELQQEKEELMQELSSLE H:  MSPEVALNRISPMLSPFISSVVRNGKVGLDATNCLRITDL KSGCTSLTPGPNCDRFKLHIPYAGETLKWDIIFNAQYPEL PPDFIFGEDAEFLPDPSALQNLASWNPSNPECLLLVVKEL VQQYHQFQCSRLRESSRLMFEYQTLLEEPQYGENMEIYAG KKNNWTGEFSARFLLKLPVDFSNIPTYLLKDVNEDPGEDV ALLSVSFEDTEATQVYPKLYLSPRIEHALGGSSALHIPAF PGGGCLIDYVPQVCHLLTNKVQYVIQGYHKRREYIAAFLS HFGTGVVEYDAEGFTKLTLLLMWKDFCFLVHIDLPLFFPR DQPTLTFQSVYHFTNSGQLYSQAQKNYPYSPRWDGNEMAK RAKAYFKTFVPQFQEAAFANGKL I:  EVQIRTPRVNCPEKVIICLDLSEEMSLPKLESFNGSKTNA LNVSQKMIEMFVRTKHKIDKSHEFALVVVNDDTAWLSGLT SDPRELCSCLYDLETASCSTFNLEGLFSLIQQKTELPVTE NVQTIPPPYVVRTILVYSRPPCQPQFSLTEPMKKMFQCPY FFFDVVYIHNGTEEKEEEMSWKDMFAFMGSLDTKGTSYKY EVALAGPALELHNCMAKLLAHPLQRPCQSHASYSLLE J:  WTGQESLSDSDPEMWELLQREKDRQCRGLELIASENFCSR AALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRR ALEAFDLDPAQWGVNVQPYSGSPANLAVYTALLQPHDRIM GLDLSIFFESMPYKLNPKTGLIDYNQLALTARLFRPRLII AGTSAYARLIDYARMREVCDEVKAHLLADMAHISGLVAAK VIPSPFKHADIVTTTTHKTLRGTRSGLIFYRKGVKAVDPK TGREIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQA CTPMFREYSLQVLKNARAMADALLERGYSLVSGGTDNHLV LVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPG GLRLGAPALTSRQFREDDFRRVVDFIDEGVNIGLEVKSKT AKLQDFKSFLLKDSETSQRLANLRQRVEQFARAFPMPGFD Description Functional site 1) chain B residue 122 type sequence H description binding site for residue ZN B 401 source : AC1 2) chain B residue 124 type sequence H description binding site for residue ZN B 401 source : AC1 3) chain B residue 135 type sequence D description binding site for residue ZN B 401 source : AC1 4) chain G residue 122 type sequence H description binding site for residue ZN G 401 source : AC2 5) chain G residue 124 type sequence H description binding site for residue ZN G 401 source : AC2 6) chain G residue 135 type sequence D description binding site for residue ZN G 401 source : AC2 7) chain E residue 82 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI1 8) chain J residue 175 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI1 9) chain J residue 276 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI1 10) chain J residue 335 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI1 11) chain J residue 443 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI1 12) chain J residue 448 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI1 13) chain J residue 453 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI1 14) chain E residue 175 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI1 15) chain E residue 276 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI1 16) chain E residue 335 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI1 17) chain E residue 443 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI1 18) chain E residue 448 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI1 19) chain E residue 453 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI1 20) chain J residue 82 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI1 21) chain E residue 259 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:29180469 source Swiss-Prot : SWS_FT_FI2 22) chain J residue 259 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:29180469 source Swiss-Prot : SWS_FT_FI2 23) chain E residue 449 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 24) chain J residue 449 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3

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