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PDBsum entry 1wr3

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protein links
Ligase PDB id
1wr3

 

 

 

 

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Contents
Protein chain
36 a.a. *
* Residue conservation analysis
PDB id:
1wr3
Name: Ligase
Title: Solution structure of the first ww domain of nedd4-2
Structure: Ubiquitin-protein ligase nedd4-2. Chain: a. Fragment: first ww domain. Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
NMR struc: 20 models
Authors: K.Kowalski,A.L.Merkel,G.W.Booker
Key ref: K.Kowalski et al. Solution structures of ww domains of nedd4-2. To be published, .
Date:
11-Oct-04     Release date:   18-Oct-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q8CFI0  (NED4L_MOUSE) -  E3 ubiquitin-protein ligase NEDD4-like from Mus musculus
Seq:
Struc:
 
Seq:
Struc:
1004 a.a.
36 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 1: E.C.2.3.2.26  - HECT-type E3 ubiquitin transferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6- ubiquitinyl-[acceptor protein]-L-lysine
   Enzyme class 2: E.C.2.3.2.36  - RING-type E3 ubiquitin transferase (cysteine targeting).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

 

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