4PQT

Insights into the mechanism of deubiquitination by JAMM deubiquitinases from co-crystal structures of enzyme with substrate and product

Entity

Entity ID	Chain ID	Description	Type	Chain length	Formula weight	Number of molecules	DB Name (Accession)	Biological source	Descriptive keywords
1	A (A)	AMSH-like protease sst2	polymer	197	21937.7	1	UniProt (Q9P371) Pfam (PF01398)	Schizosaccharomyces pombe (Fission yeast)	Suppressor of ste12 deletion protein 2
2	B (B)	Protein UBBP4	polymer	81	8988.3	1	UniProt (J3QRK5)	Homo sapiens (human)
3	C (A)	ZINC ION	non-polymer		65.4	1	Chemie (ZN)
4	D, E, F (A, B)	1,2-ETHANEDIOL	non-polymer		62.1	3	Chemie (EDO)
5	G, H (A, B)	water	water		18.0	78	Chemie (HOH)

Sequence modifications

A: 245 - 435 (UniProt: Q9P371)

PDB	External Database	Details
Gly 239	-	expression tag
Pro 240	-	expression tag
Leu 241	-	expression tag
Gly 242	-	expression tag
Ser 243	-	expression tag
Met 244	-	expression tag
Ala 354	Asp 354	engineered mutation

B: 1 - 76 (UniProt: J3QRK5)

PDB	External Database	Details
Gly -4	-	expression tag
Pro -3	-	expression tag
Leu -2	-	expression tag
Gly -1	-	expression tag
Ser 0	-	expression tag
Thr 55	Ser 131	conflict

Contents of the asymmetric unit

Polymers	Number of chains	2
	Total formula weight	30926.0
Non-Polymers*	Number of molecules	4
	Total formula weight	251.6
All*	Total formula weight	31177.6

*Water molecules are not included.