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4PQT

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

Entity
Entity IDChain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
1A
(A)
AMSH-like protease sst2polymer19721937.71UniProt (Q9P371)
Pfam (PF01398)
Schizosaccharomyces pombe (Fission yeast)Suppressor of ste12 deletion protein 2
2B
(B)
Protein UBBP4polymer818988.31UniProt (J3QRK5)Homo sapiens (human)
3C
(A)
ZINC IONnon-polymer65.41Chemie (ZN)
4D, E, F
(A, B)
1,2-ETHANEDIOLnon-polymer62.13Chemie (EDO)
5G, H
(A, B)
waterwater18.078Chemie (HOH)
Sequence modifications
A: 245 - 435 (UniProt: Q9P371)
PDBExternal DatabaseDetails
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 354Asp 354engineered mutation
B: 1 - 76 (UniProt: J3QRK5)
PDBExternal DatabaseDetails
Gly -4-expression tag
Pro -3-expression tag
Leu -2-expression tag
Gly -1-expression tag
Ser 0-expression tag
Thr 55Ser 131conflict
Sequence viewer
Contents of the asymmetric unit
PolymersNumber of chains2
Total formula weight30926.0
Non-Polymers*Number of molecules4
Total formula weight251.6
All*Total formula weight31177.6
*Water molecules are not included.

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PDB entries from 2024-11-06

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