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PDBsum entry 3v31

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protein metals Protein-protein interface(s) links
Protein binding PDB id
3v31
Jmol
Contents
Protein chains
166 a.a.
18 a.a.
Metals
_NA ×2
_CL
Waters ×139
PDB id:
3v31
Name: Protein binding
Title: Crystal structure of the peptide bound complex of the ankyri domains of human ankra2
Structure: Ankyrin repeat family a protein 2. Chain: a. Fragment: unp residues 148-313 (ank repeats). Synonym: rfxank-like protein 2. Engineered: yes. Histone deacetylase 4. Chain: b. Synonym: hd4. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ankra, ankra2. Expressed in: escherichia coli. Expression_system_taxid: 469008. Synthetic: yes. Other_details: this sequence occurs naturally in human hdac
Resolution:
1.57Å     R-factor:   0.176     R-free:   0.204
Authors: R.Lam,C.Xu,C.B.Bian,J.Kania,C.Bountra,J.Weigelt,C.H.Arrowsmi A.M.Edwards,A.Bochkarev,J.Min,Structural Genomics Consortiu
Key ref: C.Xu et al. (2012). Sequence-specific recognition of a PxLPxI/L motif by an ankyrin repeat tumbler lock. Sci Signal, 5, ra39. PubMed id: 22649097 DOI: 10.1126/scisignal.2002979
Date:
12-Dec-11     Release date:   04-Apr-12    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9H9E1  (ANRA2_HUMAN) -  Ankyrin repeat family A protein 2
Seq:
Struc:
313 a.a.
166 a.a.*
Protein chain
Pfam   ArchSchema ?
P56524  (HDAC4_HUMAN) -  Histone deacetylase 4
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1084 a.a.
17 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: Chain B: E.C.3.5.1.98  - Histone deacetylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1126/scisignal.2002979 Sci Signal 5:ra39 (2012)
PubMed id: 22649097  
 
 
Sequence-specific recognition of a PxLPxI/L motif by an ankyrin repeat tumbler lock.
C.Xu, J.Jin, C.Bian, R.Lam, R.Tian, R.Weist, L.You, J.Nie, A.Bochkarev, W.Tempel, C.S.Tan, G.A.Wasney, M.Vedadi, G.D.Gish, C.H.Arrowsmith, T.Pawson, X.J.Yang, J.Min.
 
  ABSTRACT  
 
No abstract given.