5OHN

Crystal structure of USP30 in covalent complex with ubiquitin propargylamide (low resolution)

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, C)	Ubiquitin carboxyl-terminal hydrolase 30,Ubiquitin carboxyl-terminal hydrolase 30	polymer	370	42582.0	2	UniProt (Q70CQ3) Pfam (PF00443)	Homo sapiens (Human)	Deubiquitinating enzyme 30,Ubiquitin thioesterase 30,Ubiquitin-specific-processing protease 30,Ub-specific protease 30,Deubiquitinating enzyme 30,Ubiquitin thioesterase 30,Ubiquitin-specific-processing protease 30,Ub-specific protease 30
2	B, D (B, D)	Polyubiquitin-B	polymer	76	8558.9	2	UniProt (P0CG47) Pfam (PF00240)	Homo sapiens (Human)
3	E, F (A, C)	ZINC ION	non-polymer		65.4	2	Chemie (ZN)

Sequence modifications

A, C: 64 - 357 (UniProt: Q70CQ3)

PDB	External Database	Details
Gly 62	-	expression tag
Pro 63	-	expression tag
Asp 348	Phe 348	engineered mutation
Asp 350	Met 350	engineered mutation
Glu 353	Ile 353	engineered mutation

A, C: 432 - 502 (UniProt: Q70CQ3)

PDB	External Database	Details
Ser 358	-	linker
Asn 359	-	linker
Ala 360	-	linker

B, D: 1 - 76 (UniProt: P0CG47)

PDB	External Database	Details
Aye 76	Gly 76	engineered mutation

Contents of the asymmetric unit

Polymers	Number of chains	4
	Total formula weight	102281.8
Non-Polymers*	Number of molecules	2
	Total formula weight	130.8
All*	Total formula weight	102412.6

*Water molecules are not included.