eF-site ID 6n3p-H PDB Code 6n3p Chain H click to enlarge Title Crosslinked AcpP=FabZ complex from E. coli Type II FAS Classification BIOSYNTHETIC PROTEIN Compound 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ Source (ACP_ECO45) Sequence H:  TIEERVKKIIGEQLGVKQEEVTNNASFVEDLGADSLDTVE LVMALEEEFDTEIPDEEAEKITTVQAAIDYINGHQ Description Functional site 1) chain H residue 70 type sequence D description binding site for Di-peptide XLN B 400 and SER K 36 source : AC3 2) chain H residue 70 type sequence D description binding site for Di-peptide XLN B 400 and SER K 36 source : AC4 3) chain H residue 35 type sequence D description binding site for Di-peptide XLN D 400 and SER H 36 source : AC9 4) chain H residue 37 type sequence L description binding site for Di-peptide XLN D 400 and SER H 36 source : AC9 5) chain H residue 38 type sequence D description binding site for Di-peptide XLN D 400 and SER H 36 source : AC9 6) chain H residue 39 type sequence T description binding site for Di-peptide XLN D 400 and SER H 36 source : AC9 7) chain H residue 40 type sequence V description binding site for Di-peptide XLN D 400 and SER H 36 source : AC9 8) chain H residue 35 type sequence D description binding site for Di-peptide XLN D 400 and SER H 36 source : AD1 9) chain H residue 37 type sequence L description binding site for Di-peptide XLN D 400 and SER H 36 source : AD1 10) chain H residue 38 type sequence D description binding site for Di-peptide XLN D 400 and SER H 36 source : AD1 11) chain H residue 39 type sequence T description binding site for Di-peptide XLN D 400 and SER H 36 source : AD1 12) chain H residue 40 type sequence V description binding site for Di-peptide XLN D 400 and SER H 36 source : AD1 13) chain H residue 36 type sequence S description binding site for Di-peptide XLN D 400 and HIS D 54 source : AD2 14) chain H residue 36 type sequence S description binding site for Di-peptide XLN D 400 and HIS D 54 source : AD3 15) chain H residue 36 type MOD_RES sequence S description O-(pantetheine 4'-phosphoryl)serine => ECO:0000255|PROSITE-ProRule:PRU00258, ECO:0000269|PubMed:4882207 source Swiss-Prot : SWS_FT_FI1

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