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PDBsum entry 3v6c

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protein ligands metals Protein-protein interface(s) links
Hydrolase/signaling protein PDB id
3v6c

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
327 a.a.
81 a.a.
Ligands
GOL
Metals
_ZN
_CL ×2
Waters ×291
PDB id:
3v6c
Name: Hydrolase/signaling protein
Title: Crystal structure of usp2 in complex with mutated ubiquitin
Structure: Ubiquitin carboxyl-terminal hydrolase 2. Chain: a. Synonym: 41 kda ubiquitin-specific protease, deubiquitinating enzyme 2, ubiquitin thiolesterase 2, ubiquitin-specific-processing protease 2. Engineered: yes. Ubiquitin. Chain: b. Engineered: yes.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ubp41, usp02.258.605, usp2. Expressed in: escherichia coli. Expression_system_taxid: 469008. Gene: ubc.
Resolution:
1.70Å     R-factor:   0.178     R-free:   0.220
Authors: M.Neculai,A.Ernst,S.Sidhu,C.H.Arrowsmith,A.M.Edwards,C.Bountra, J.Weigelt,S.Dhe-Paganon,Structural Genomics Consortium (Sgc)
Key ref: M.Neculai et al. Crystal structure of usp2 in complex with mutated ubi. To be published, .
Date:
19-Dec-11     Release date:   19-Dec-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
O75604  (UBP2_HUMAN) -  Ubiquitin carboxyl-terminal hydrolase 2 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
605 a.a.
327 a.a.
Protein chain
Pfam   ArchSchema ?
P0CG48  (UBC_HUMAN) -  Polyubiquitin-C from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
685 a.a.
81 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 7 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 2: 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).
   Enzyme class 3: Chain B: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
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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