eF-site ID 6ae8-B PDB Code 6ae8 Chain B click to enlarge Title Structure insight into histone chaperone Chz1-mediated H2A.Z recognition and replacement Classification CHAPERONE Compound Histone H2B.1,Histone H2A.Z Source (CHZ1_YEAST) Sequence B:  MRKETYSSYIYKVLKQTHPDTGISQKSMSILNSFVNDIFE RIATEASKLAAYNKKSTISAREIQTAVRLILPGELAKHAV SEGTRAVTKYSSSTQAQSSSARAGLQFPVGRIKRYLKRHA TGRTRVGSKAAIYLTAVLEYLTAEVLELAGNAAKDLKVKR ITPRHLQLAIRGDDELDSLIRA Description Functional site 1) chain B residue 0 type sequence M description binding site for residue BCN B 201 source : AC2 2) chain B residue 1 type sequence R description binding site for residue BCN B 201 source : AC2 3) chain B residue 2 type sequence K description binding site for residue BCN B 201 source : AC2 4) chain B residue 5 type sequence Y description binding site for residue BCN B 201 source : AC2 5) chain B residue 35 type sequence N description binding site for residue BCN B 201 source : AC2 6) chain B residue 38 type sequence F description binding site for residue BCN B 201 source : AC2 7) chain B residue 39 type sequence E description binding site for residue BCN B 201 source : AC2 8) chain B residue 114 type sequence Y description binding site for residue BCN B 201 source : AC2 9) chain B residue 117 type sequence R description binding site for residue BCN B 201 source : AC2 10) chain B residue 11 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI2 11) chain B residue 88 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:10642555, ECO:0000269|PubMed:12535538, ECO:0000269|PubMed:12535539, ECO:0000269|PubMed:14660635, ECO:0000269|PubMed:15280549, ECO:0000269|PubMed:16432255 source Swiss-Prot : SWS_FT_FI3

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