5XIS

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

Entity

Entity ID	Chain ID	Description	Type	Chain length	Formula weight	Number of molecules	DB Name (Accession)	Biological source	Descriptive keywords
1	A, D (A, D)	E3 ubiquitin-protein ligase RNF168	polymer	84	9947.9	2	UniProt (Q8IYW5)	Homo sapiens (Human)	hRNF168,RING finger protein 168,RING-type E3 ubiquitin transferase RNF168
2	B, E (B, E)	Ubiquitin-40S ribosomal protein S27a	polymer	77	8691.9	2	UniProt (P62983) Pfam (PF00240)	Mus musculus (Mouse)	Ubiquitin carboxyl extension protein 80
3	C, F (C, F)	Ubiquitin-40S ribosomal protein S27a	polymer	76	8604.8	2	UniProt (P62983) Pfam (PF00240)	Mus musculus (Mouse)	Ubiquitin carboxyl extension protein 80
4	G, J (A, D)	beta-D-xylofuranose	non-polymer		150.1	2	Chemie (XYZ)
5	H, I (B, C)	MAGNESIUM ION	non-polymer		24.3	2	Chemie (MG)
6	K, L, M, N, O... (A, B, C, D, E...)	water	water		18.0	312	Chemie (HOH)

Sequence modifications

A, D: 110 - 188 (UniProt: Q8IYW5)

PDB	External Database	Details
Gly 105	-	expression tag
Pro 106	-	expression tag
Gly 107	-	expression tag
His 108	-	expression tag
Met 109	-	expression tag

B, E: 1 - 76 (UniProt: P62983)

PDB	External Database	Details
Asp 77	-	see sequence details

C, F: 1 - 76 (UniProt: P62983)

PDB	External Database	Details
Arg 63	Lys 63	engineered mutation

Contents of the asymmetric unit

Polymers	Number of chains	6
	Total formula weight	54489.4
Non-Polymers*	Number of molecules	4
	Total formula weight	348.9
All*	Total formula weight	54838.2

*Water molecules are not included.