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PDBsum entry 5l8h

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protein metals Protein-protein interface(s) links
Hydrolase PDB id
5l8h

 

 

 

 

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Contents
Protein chains
311 a.a.
76 a.a.
Metals
_ZN
Waters ×250
PDB id:
5l8h
Name: Hydrolase
Title: Structure of usp46-ubvme
Structure: Ubiquitin carboxyl-terminal hydrolase 46. Chain: a. Synonym: deubiquitinating enzyme 46,ubiquitin thioesterase 46, ubiquitin-specific-processing protease 46. Engineered: yes. Polyubiquitin-b. Chain: b. Engineered: yes. Other_details: recombinant expression followed by chemical synthesis.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: usp46. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: ubb. Expression_system_taxid: 562
Resolution:
1.85Å     R-factor:   0.168     R-free:   0.194
Authors: M.Clerici,T.Sixma,S.Dharadhar
Key ref: S.Dharadhar et al. (2016). A conserved two-step binding for the UAF1 regulator to the USP12 deubiquitinating enzyme. J Struct Biol, 196, 437-447. PubMed id: 27650958 DOI: 10.1016/j.jsb.2016.09.011
Date:
07-Jun-16     Release date:   28-Sep-16    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P62068  (UBP46_HUMAN) -  Ubiquitin carboxyl-terminal hydrolase 46 from Homo sapiens
Seq:
Struc:
366 a.a.
311 a.a.*
Protein chain
Pfam   ArchSchema ?
P0CG47  (UBB_HUMAN) -  Polyubiquitin-B from Homo sapiens
Seq:
Struc:
229 a.a.
76 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chain A: E.C.3.4.19.12  - ubiquitinyl hydrolase 1.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Thiol-dependent hydrolysis of ester, thiolester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

 

 
DOI no: 10.1016/j.jsb.2016.09.011 J Struct Biol 196:437-447 (2016)
PubMed id: 27650958  
 
 
A conserved two-step binding for the UAF1 regulator to the USP12 deubiquitinating enzyme.
S.Dharadhar, M.Clerici, W.J.van Dijk, A.Fish, T.K.Sixma.
 
  ABSTRACT  
 
No abstract given.

 

 

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