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PDBsum entry 4v1c

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
4v1c

 

 

 

 

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Contents
Protein chains
270 a.a.
252 a.a.
191 a.a.
Ligands
ARG-THR-BTK-GLN-
THR-ALA-ARG
×6
GOL ×6
Metals
_ZN ×5
Obsolete entry
PDB id:
4v1c
Name: Hydrolase
Title: Sirtuin 3
Structure: NAD-dependent protein deacetylase sirtuin-3, mitochondrial. Chain: a. Fragment: catalytic domain, unp residues 121-394. Synonym: hsirt3, regulatory protein sir2 homolog 3, sir2-like protein 3, sirt6. Engineered: yes. NAD-dependent protein deacetylase sirtuin-3, mitochondrial. Chain: b, e, g, k. Fragment: catalytic domain, unp residues 121-394.
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: rosetta. Synthetic construct. Organism_taxid: 32630.
Resolution:
2.95Å     R-factor:   0.227     R-free:   0.278
Authors: Y.Wang,Q.Hao
Key ref: X.Bao et al. (2014). Identification of 'erasers' for lysine crotonylated histone marks using a chemical proteomics approach. Elife, 3, . PubMed id: 25369635 DOI: 10.7554/eLife.02999
Date:
25-Sep-14     Release date:   12-Nov-14    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9NTG7  (SIR3_HUMAN) -  NAD-dependent protein deacetylase sirtuin-3, mitochondrial from Homo sapiens
Seq:
Struc:
399 a.a.
270 a.a.*
Protein chains
Pfam   ArchSchema ?
Q9NTG7  (SIR3_HUMAN) -  NAD-dependent protein deacetylase sirtuin-3, mitochondrial from Homo sapiens
Seq:
Struc:
399 a.a.
252 a.a.
Protein chain
Pfam   ArchSchema ?
Q9NTG7  (SIR3_HUMAN) -  NAD-dependent protein deacetylase sirtuin-3, mitochondrial from Homo sapiens
Seq:
Struc:
399 a.a.
191 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: Chains A, B, E, I: E.C.3.5.1.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.7554/eLife.02999 Elife 3: (2014)
PubMed id: 25369635  
 
 
Identification of 'erasers' for lysine crotonylated histone marks using a chemical proteomics approach.
X.Bao, Y.Wang, X.Li, X.M.Li, Z.Liu, T.Yang, C.F.Wong, J.Zhang, Q.Hao, X.D.Li.
 
  ABSTRACT  
 
No abstract given.

 

 

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