9V6Q

Cryo-EM structure of two cPRC1 complexes bound to opposite faces of an endogenous 147-bp mono-nucleosome

Entity

Entity ID	Chain ID	Description	Type	Chain length	Formula weight	Number of molecules	DB Name (Accession)	Biological source	Descriptive keywords
1	A, C (A, E)	Histone H3.1	polymer	136	15437.2	2	UniProt (P68431)	Homo sapiens (human)	Histone H3/a,Histone H3/b,Histone H3/c,Histone H3/d,Histone H3/f,Histone H3/h,Histone H3/i,Histone H3/j,Histone H3/k,Histone H3/l
2	B, E (G, C)	Histone H2A type 1-H	polymer	128	13935.3	2	UniProt (Q96KK5)	Homo sapiens (human)	H2A-clustered histone 12,Histone H2A/s
3	D, F (D, H)	Histone H2B type 1-C/E/F/G/I	polymer	126	13937.2	2	UniProt (P62807)	Homo sapiens (human)	Histone H2B.1 A,Histone H2B.a,H2B/a,Histone H2B.g,H2B/g,Histone H2B.h,H2B/h,Histone H2B.k,H2B/k,Histone H2B.l,H2B/l
4	G, H (B, F)	Histone H4	polymer	103	11394.4	2	UniProt (P62805)	Homo sapiens (human)
5	I (I)	DNA (144-MER)	polymer	144	44217.2	1		Homo sapiens
6	J (J)	DNA (145-MER)	polymer	145	44992.6	1		Homo sapiens
7	K, M (M, K)	Polycomb complex protein BMI-1	polymer	326	37006.1	2	UniProt (P35226)	Homo sapiens (human)	Polycomb group RING finger protein 4,RING finger protein 51
8	L, N (N, L)	E3 ubiquitin-protein ligase RING2	polymer	336	37706.4	2	UniProt (Q99496)	Homo sapiens (human)	Huntingtin-interacting protein 2-interacting protein 3,HIP2-interacting protein 3,Protein DinG,RING finger protein 1B,RING1b,RING finger protein 2,RING finger protein BAP-1,RING-type E3 ubiquitin transferase RING2
9	O, P, Q, R, S... (M, N, K, L)	ZINC ION	non-polymer		65.4	8	Chemie (ZN) PubChem (32051)

Contents of the asymmetric unit

Polymers	Number of chains	14
	Total formula weight	348042.9
Non-Polymers*	Number of molecules	8
	Total formula weight	523.3
All*	Total formula weight	348566.2

*Water molecules are not included.