eF-site ID 6iwq-ABCDEF PDB Code 6iwq Chain A, B, C, D, E, F Title Crystal structure of GalNAc-T7 with Mn2+ Classification TRANSFERASE Compound N-acetylgalactosaminyltransferase 7 Source (GALT7_HUMAN) Sequence A:  YLTFKPQTFTYHDPVLRPGILGNFEPKEPEPPGVVGGPGE KAKPLVLGPEFKQAIQASIKEFGFNMVASDMISLDRSVND LRQEECKYWHYDENLLTSSVVIVFHNEGWSTLMRTVHSVI KRTPRKYLAEIVLIDDFSNKEHLKEKLDEYIKLWNGLVKV FRNERREGLIQARSIGAQKAKLGQVLIYLDAHCEVAVNWY APLVAPISKDRTICTVPLIDVINGNTYEIIPQGGGDEDGY ARGAWDWSMLWKRVPLTPQEKRLRKTKTEPYRSPAMAGGL FAIEREFFFELGLYDPGLQIWGGENFEISYKIWQCGGKLL FVPCSRVGHIYRLEGWQGNPPPIYVGSSPTLKNYVRVVEV WWDEYKDYFYASRPESQALPYGDISELKKFREDHNCKSFK WFMEEIAYDITSHYPLPPKNVDWGEIRGFETAYCIDSMGK TNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGAD GSKVMITHCNLNEFKEWQYFKNLHRFTHIPSGKCLDRSEV LHQVFISNCDSSKTTQKWEMNNIHSV B:  YLTFKPQTFTYHDPVLRPGILGNFEPKEPEPPGVVGGPGE KAKPLVLGPEFKQAIQASIKEFGFNMVASDMISLDRSVND LRQEECKYWHYDENLLTSSVVIVFHNEGWSTLMRTVHSVI KRTPRKYLAEIVLIDDFSNKEHLKEKLDEYIKLWNGLVKV FRNERREGLIQARSIGAQKAKLGQVLIYLDAHCEVAVNWY APLVAPISKDRTICTVPLIDVINGNTYEIIPQGGGDEDGY ARGAWDWSMLWKRVPLTPQEKRLRKTKTEPYRSPAMAGGL FAIEREFFFELGLYDPGLQIWGGENFEISYKIWQCGGKLL FVPCSRVGHIYRLEGWQGNPPPIYVGSSPTLKNYVRVVEV WWDEYKDYFYASRPESQALPYGDISELKKFREDHNCKSFK WFMEEIAYDITSHYPLPPKNVDWGEIRGFETAYCIDSMGK TNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGAD GSKVMITHCNLNEFKEWQYFKNLHRFTHIPSGKCLDRSEV LHQVFISNCDSSKTTQKWEMNNIHSV C:  YLTFKPQTFTYHDPVLRPGILGNFEPKEPEPPGVVGGPGE KAKPLVLGPEFKQAIQASIKEFGFNMVASDMISLDRSVND LRQEECKYWHYDENLLTSSVVIVFHNEGWSTLMRTVHSVI KRTPRKYLAEIVLIDDFSNKEHLKEKLDEYIKLWNGLVKV FRNERREGLIQARSIGAQKAKLGQVLIYLDAHCEVAVNWY APLVAPISKDRTICTVPLIDVINGNTYEIIPQGGGDEDGY ARGAWDWSMLWKRVPLTPQEKRLRKTKTEPYRSPAMAGGL FAIEREFFFELGLYDPGLQIWGGENFEISYKIWQCGGKLL FVPCSRVGHIYRLEGWQGNPPPIYVGSSPTLKNYVRVVEV WWDEYKDYFYASRPESQALPYGDISELKKFREDHNCKSFK WFMEEIAYDITSHYPLPPKNVDWGEIRGFETAYCIDSMGK TNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGAD GSKVMITHCNLNEFKEWQYFKNLHRFTHIPSGKCLDRSEV LHQVFISNCDSSKTTQKWEMNNIHSV D:  YLTFKPQTFTYHDPVLRPGILGNFEPKEPEPPGVVGGPGE KAKPLVLGPEFKQAIQASIKEFGFNMVASDMISLDRSVND LRQEECKYWHYDENLLTSSVVIVFHNEGWSTLMRTVHSVI KRTPRKYLAEIVLIDDFSNKEHLKEKLDEYIKLWNGLVKV FRNERREGLIQARSIGAQKAKLGQVLIYLDAHCEVAVNWY APLVAPISKDRTICTVPLIDVINGNTYEIIPQGGGDEDGY ARGAWDWSMLWKRVPLTPQEKRLRKTKTEPYRSPAMAGGL FAIEREFFFELGLYDPGLQIWGGENFEISYKIWQCGGKLL FVPCSRVGHIYRLEGWQGNPPPIYVGSSPTLKNYVRVVEV WWDEYKDYFYASRPESQALPYGDISELKKFREDHNCKSFK WFMEEIAYDITSHYPLPPKNVDWGEIRGFETAYCIDSMGK TNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGAD GSKVMITHCNLNEFKEWQYFKNLHRFTHIPSGKCLDRSEV LHQVFISNCDSSKTTQKWEMNNIHSV E:  YLTFKPQTFTYHDPVLRPGILGNFEPKEPEPPGVVGGPGE KAKPLVLGPEFKQAIQASIKEFGFNMVASDMISLDRSVND LRQEECKYWHYDENLLTSSVVIVFHNEGWSTLMRTVHSVI KRTPRKYLAEIVLIDDFSNKEHLKEKLDEYIKLWNGLVKV FRNERREGLIQARSIGAQKAKLGQVLIYLDAHCEVAVNWY APLVAPISKDRTICTVPLIDVINGNTYEIIPQGGGDEDGY ARGAWDWSMLWKRVPLTPQEKRLRKTKTEPYRSPAMAGGL FAIEREFFFELGLYDPGLQIWGGENFEISYKIWQCGGKLL FVPCSRVGHIYRLEGWQGNPPPIYVGSSPTLKNYVRVVEV WWDEYKDYFYASRPESQALPYGDISELKKFREDHNCKSFK WFMEEIAYDITSHYPLPPKNVDWGEIRGFETAYCIDSMGK TNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGAD GSKVMITHCNLNEFKEWQYFKNLHRFTHIPSGKCLDRSEV LHQVFISNCDSSKTTQKWEMNNIHSV F:  YLTFKPQTFTYHDPVLRPGILGNFEPKEPEPPGVVGGPGE KAKPLVLGPEFKQAIQASIKEFGFNMVASDMISLDRSVND LRQEECKYWHYDENLLTSSVVIVFHNEGWSTLMRTVHSVI KRTPRKYLAEIVLIDDFSNKEHLKEKLDEYIKLWNGLVKV FRNERREGLIQARSIGAQKAKLGQVLIYLDAHCEVAVNWY APLVAPISKDRTICTVPLIDVINGNTYEIIPQGGGDEDGY ARGAWDWSMLWKRVPLTPQEKRLRKTKTEPYRSPAMAGGL FAIEREFFFELGLYDPGLQIWGGENFEISYKIWQCGGKLL FVPCSRVGHIYRLEGWQGNPPPIYVGSSPTLKNYVRVVEV WWDEYKDYFYASRPESQALPYGDISELKKFREDHNCKSFK WFMEEIAYDITSHYPLPPKNVDWGEIRGFETAYCIDSMGK TNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGAD GSKVMITHCNLNEFKEWQYFKNLHRFTHIPSGKCLDRSEV LHQVFISNCDSSKTTQKWEMNNIHSV Description (1)  N-acetylgalactosaminyltransferase 7 (E.C.2.4.1.-) Functional site 1) chain A residue 301 type sequence D description binding site for residue MN A 701 source : AC1 2) chain A residue 303 type sequence H description binding site for residue MN A 701 source : AC1 3) chain A residue 440 type sequence H description binding site for residue MN A 701 source : AC1 4) chain B residue 301 type sequence D description binding site for residue MN B 701 source : AC2 5) chain B residue 303 type sequence H description binding site for residue MN B 701 source : AC2 6) chain B residue 440 type sequence H description binding site for residue MN B 701 source : AC2 7) chain C residue 301 type sequence D description binding site for residue MN C 701 source : AC3 8) chain C residue 303 type sequence H description binding site for residue MN C 701 source : AC3 9) chain C residue 440 type sequence H description binding site for residue MN C 701 source : AC3 10) chain D residue 301 type sequence D description binding site for residue MN D 701 source : AC4 11) chain D residue 440 type sequence H description binding site for residue MN D 701 source : AC4 12) chain E residue 301 type sequence D description binding site for residue MN E 701 source : AC5 13) chain E residue 303 type sequence H description binding site for residue MN E 701 source : AC5 14) chain E residue 440 type sequence H description binding site for residue MN E 701 source : AC5 15) chain F residue 301 type sequence D description binding site for residue MN F 701 source : AC6 16) chain F residue 303 type sequence H description binding site for residue MN F 701 source : AC6 17) chain F residue 440 type sequence H description binding site for residue MN F 701 source : AC6 18) chain C residue 412 type BINDING sequence W description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 19) chain C residue 440 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 20) chain C residue 443 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 21) chain D residue 247 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 22) chain D residue 277 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 23) chain D residue 301 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 24) chain D residue 303 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 25) chain D residue 412 type BINDING sequence W description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 26) chain D residue 440 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 27) chain D residue 443 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 28) chain E residue 247 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 29) chain E residue 277 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 30) chain E residue 301 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 31) chain E residue 303 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 32) chain E residue 412 type BINDING sequence W description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 33) chain E residue 440 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 34) chain E residue 443 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 35) chain F residue 247 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 36) chain F residue 277 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 37) chain F residue 301 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 38) chain F residue 303 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 39) chain F residue 412 type BINDING sequence W description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 40) chain F residue 440 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 41) chain F residue 443 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 42) chain C residue 303 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 43) chain A residue 277 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 44) chain A residue 301 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 45) chain A residue 303 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 46) chain A residue 412 type BINDING sequence W description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 47) chain A residue 440 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 48) chain A residue 443 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 49) chain B residue 247 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 50) chain B residue 277 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 51) chain A residue 247 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 52) chain B residue 301 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 53) chain B residue 303 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 54) chain B residue 412 type BINDING sequence W description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 55) chain B residue 440 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 56) chain B residue 443 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 57) chain C residue 247 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 58) chain C residue 277 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 59) chain C residue 301 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1

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