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PDBsum entry 3ehv

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protein metals Protein-protein interface(s) links
Ligase PDB id
3ehv

 

 

 

 

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Contents
Protein chains
70 a.a. *
Metals
_ZN
Waters ×127
* Residue conservation analysis
PDB id:
3ehv
Name: Ligase
Title: X-ray structure of human ubiquitin zn(ii) adduct
Structure: Ubiquitin. Chain: a, b, c. Engineered: yes
Source: Homo sapiens. Organism_taxid: 9606. Gene: rps27a, uba80, ubcep1, uba52, ubcep2, ubb, ubc. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.81Å     R-factor:   0.222     R-free:   0.271
Authors: G.Falini,S.Fermani,G.Tosi
Key ref: G.Falini et al. (2008). Structural probing of Zn(II), Cd(II) and Hg(II) binding to human ubiquitin. Chem Commun (camb), 45, 5960-5962. PubMed id: 19030552
Date:
15-Sep-08     Release date:   17-Mar-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P0CG48  (UBC_HUMAN) -  Polyubiquitin-C from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
685 a.a.
70 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.6.3.2.19  - Transferred entry: 2.3.2.23, 2.3.2.27 and 6.2.1.45.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine
ATP
+ ubiquitin
+ protein lysine
= AMP
+ diphosphate
+ protein N-ubiquityllysine
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Chem Commun (camb) 45:5960-5962 (2008)
PubMed id: 19030552  
 
 
Structural probing of Zn(II), Cd(II) and Hg(II) binding to human ubiquitin.
G.Falini, S.Fermani, G.Tosi, F.Arnesano, G.Natile.
 
  ABSTRACT  
 
A structural investigation performed on adducts of human ubiquitin with group-12 metal ions reveals common preferential anchoring sites, the most populated one being His68; at higher metal ion concentration a second and a third site, close to the N-terminus of the protein, become populated and promote a polymorphic transition from orthorhombic to cubic form; Glu16 and Glu18, involved in the latter metal binding, undergo a remarkable displacement from their position in native ubiquitin; the aggregate stereochemistry appears to be driven by the clustering of deshielded backbone hydrogen-bond patches, and metal ions foster this process.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21268159 F.Arnesano, B.D.Belviso, R.Caliandro, G.Falini, S.Fermani, G.Natile, and D.Siliqi (2011).
Crystallographic analysis of metal-ion binding to human ubiquitin.
  Chemistry, 17, 1569-1578.
PDB codes: 3n30 3n32
21450271 F.Miskevich, A.Davis, P.Leeprapaiwong, V.Giganti, N.M.Kostić, and L.A.Angel (2011).
Metal complexes as artificial proteases in proteomics: a palladium(II) complex cleaves various proteins in solutions containing detergents.
  J Inorg Biochem, 105, 675-683.  
19731378 S.D.Weeks, K.C.Grasty, L.Hernandez-Cuebas, and P.J.Loll (2009).
Crystal structures of Lys-63-linked tri- and di-ubiquitin reveal a highly extended chain architecture.
  Proteins, 77, 753-759.
PDB codes: 3h7p 3h7s
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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