5YDK

Crystal structure of RNF168 UDM1 in complex with Lys63-linked diubiquitin, tetrameric form

Entity

Entity ID	Chain ID	Description	Type	Chain length	Formula weight	Number of molecules	DB Name (Accession)	Biological source	Descriptive keywords
1	A, D, G, J (A, G, F, L)	E3 ubiquitin-protein ligase RNF168	polymer	87	10255.2	4	UniProt (Q8IYW5)	Homo sapiens (Human)	hRNF168,RING finger protein 168,RING-type E3 ubiquitin transferase RNF168
2	B, E, H, K (B, H, E, K)	Ubiquitin-40S ribosomal protein S27a	polymer	76	8604.8	4	UniProt (P62979) Pfam (PF00240)	Homo sapiens (Human)	Ubiquitin carboxyl extension protein 80
3	C, F, I, L (D, J, C, I)	Ubiquitin-40S ribosomal protein S27a	polymer	77	8691.9	4	UniProt (P62979) Pfam (PF00240)	Homo sapiens (Human)	Ubiquitin carboxyl extension protein 80
4	M, N (J, C)	GLYCEROL	non-polymer		92.1	2	Chemie (GOL)
5	O, P, Q, R, S... (A, B, D, G, H...)	water	water		18.0	278	Chemie (HOH)

Sequence modifications

A, G, F, L: 113 - 194 (UniProt: Q8IYW5)

PDB	External Database	Details
Gly 108	-	expression tag
Pro 109	-	expression tag
Gly 110	-	expression tag
His 111	-	expression tag
Met 112	-	expression tag

B, H, E, K: 1 - 76 (UniProt: P62979)

PDB	External Database	Details
Arg 63	Lys 63	engineered mutation

D, J, C, I: 1 - 77 (UniProt: P62979)

PDB	External Database	Details
Asp 77	Ala 77	conflict

Contents of the asymmetric unit

Polymers	Number of chains	12
	Total formula weight	110207.9
Non-Polymers*	Number of molecules	2
	Total formula weight	184.2
All*	Total formula weight	110392.1

*Water molecules are not included.