eF-site ID 6fpg-BCDEFGHI PDB Code 6fpg Chain B, C, D, E, F, G, H, I click to enlarge Title Structure of the Ustilago maydis chorismate mutase 1 in complex with a Zea mays kiwellin Classification CELL INVASION Compound Chromosome 16, whole genome shotgun sequence Source (A0A1D6GNR3_MAIZE) Sequence B:  GKSEAAEIEAGDRLDALRDQLQRYETPIIQTILARSALGG RAPSEQDEVRAALSRNAFEPSEVISEWLQTESGARFRSTR PLPPAVEFITPVVLSRDTVLDKPVVGKGIFPIGRRPQDPT NMDEFLDTSLLSLNQSSTVDLASAVSLDVSLLHLVSARVL LGYPIALAKFDWLHDNFCHILTNTTLSKSQKLANIIQQLT DHKQEVNVLSRVEQKSKSLSHLFRNDIPYPPHTQDRILRL FQAYLIPITTQIEAAAILDHANKC C:  SEAAEIEAGDRLDALRDQLQRYETPIIQTILARSALGGRA PSEQDEVRAALSRNAFEPSEVISEWLQTESGARFRSTRPL PPAVEFITPVVLSRDTVLDKPVVGKGIFPIGRRPQDPTNM DEFLDTSLLSLNQSSTVDLASAVSLDVSLLHLVSARVLLG YPIALAKFDWLHDNFCHILTNTTLSKSQKLANIIQQLTDH KQEVNVLSRVEQKSKSLSHLFRNDIPYPPHTQDRILRLFQ AYLIPITTQIEAAAILDHANKC D:  TCQPSGSIQGRSGNCNECCKNGRRYTTYGCSPPVTGSTRA VLTLNSFAEGGGGAAACTGKFYDDSKKVVALSTGWYNGGS RCRKHIMIHAGNGNSVSALVVDECDSTVGCDKDHNFEPPC RNNIVDGSPAVWDALGLNKDDGQAQITWSDELE E:  TCQPSGSIQGRSGNCNTSECCKNGRRYTTYGCSPPVTGST RAVLTLNSFAEGGDGGGAAACTGKFYDDSKKVVALSTGWY NGGSRCRKHIMIHAGNGNSVSALVVDECDSTVGCDKDHNF EPPCRNNIVDGSPAVWDALGLNKDDGQAQITWSDELE F:  GKSEAAEIEAGDRLDALRDQLQRYETPIIQTILARSALGG RAPSEQDEVRAALSRNAFEPSEVISEWLQTESGARFRSTR PLPPAVEFITPVVLSRDTVLDKPVVGKGIFPIGRRPQDPT NMDEFLDTSLLSLNQSSTVDLASAVSLDVSLLHLVSARVL LGYPIALAKFDWLHDNFCHILTNTTLSKSQKLANIIQQLT DHKQEVNVLSRVEQKSKSLSHLFRNDIPYPPHTQDRILRL FQAYLIPITTQIEAAAILDHANKCTL G:  GKSEAAEIEAGDRLDALRDQLQRYETPIIQTILARSALGG RAPSEQDEVRAALSRNAFEPSEVISEWLQTESGARFRSTR PLPPAVEFITPVVLSRDTVLDKPVVGKGIFPIGRRPQDPT NMDEFLDTSLLSLNQSSTVDLASAVSLDVSLLHLVSARVL LGYPIALAKFDWLHDNFCHILTNTTLSKSQKLANIIQQLT DHKQEVNVLSRVEQKSKSLSHLFRNDIPYPPHTQDRILRL FQAYLIPITTQIEAAAILDHANKCT H:  TCQPSGSIQGRSGNCNTEECCKNGRRYTTYGCSPPVTGST RAVLTLNSFAEGGGGAAACTGKFYDDSKKVVALSTGWYNG GSRCRKHIMIHAGNGNSVSALVVDECDSTVGCDKDHNFEP PCRNNIVDGSPAVWDALGLNKDDGQAQITWSDEL I:  TCQPSGSIQGRSGNCNTSECCKNGRRYTTYGCSPPVTGST RAVLTLNSFAEGGGGAAACTGKFYDDSKKVVALSTGWYNG GSRCRKHIMIHAGNGNSVSALVVDECDSTVGCDKDHNFEP PCRNNIVDGSPAVWDALGLNKDDGQAQITWSDEL Description Functional site 1) chain C residue 43 type sequence R description binding site for residue CIT C 301 source : AC1 2) chain C residue 190 type sequence I description binding site for residue CIT C 301 source : AC1 3) chain C residue 194 type sequence K description binding site for residue CIT C 301 source : AC1 4) chain C residue 229 type sequence Q description binding site for residue CIT C 301 source : AC1 5) chain C residue 278 type sequence E description binding site for residue CIT C 301 source : AC1 6) chain E residue 160 type sequence D description binding site for residue CIT C 301 source : AC1 7) chain B residue 43 type sequence R description binding site for residue CIT B 301 source : AC2 8) chain B residue 194 type sequence K description binding site for residue CIT B 301 source : AC2 9) chain B residue 229 type sequence Q description binding site for residue CIT B 301 source : AC2 10) chain B residue 278 type sequence E description binding site for residue CIT B 301 source : AC2 11) chain D residue 160 type sequence D description binding site for residue CIT B 301 source : AC2 12) chain F residue 43 type sequence R description binding site for residue CIT F 301 source : AC3 13) chain F residue 190 type sequence I description binding site for residue CIT F 301 source : AC3 14) chain F residue 194 type sequence K description binding site for residue CIT F 301 source : AC3 15) chain F residue 229 type sequence Q description binding site for residue CIT F 301 source : AC3 16) chain F residue 278 type sequence E description binding site for residue CIT F 301 source : AC3 17) chain I residue 160 type sequence D description binding site for residue CIT F 301 source : AC3 18) chain G residue 43 type sequence R description binding site for residue CIT G 301 source : AC4 19) chain G residue 190 type sequence I description binding site for residue CIT G 301 source : AC4 20) chain G residue 194 type sequence K description binding site for residue CIT G 301 source : AC4 21) chain G residue 229 type sequence Q description binding site for residue CIT G 301 source : AC4 22) chain G residue 278 type sequence E description binding site for residue CIT G 301 source : AC4 23) chain H residue 160 type sequence D description binding site for residue CIT G 301 source : AC4 24) chain C residue 159 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 source Swiss-Prot : SWS_FT_FI1 25) chain C residue 208 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 source Swiss-Prot : SWS_FT_FI1 26) chain B residue 159 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 source Swiss-Prot : SWS_FT_FI1 27) chain B residue 208 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 source Swiss-Prot : SWS_FT_FI1 28) chain F residue 159 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 source Swiss-Prot : SWS_FT_FI1 29) chain F residue 208 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 source Swiss-Prot : SWS_FT_FI1 30) chain G residue 159 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 source Swiss-Prot : SWS_FT_FI1 31) chain G residue 208 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 source Swiss-Prot : SWS_FT_FI1

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