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PDBsum entry 1pvb

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protein ligands metals links
Calcium binding protein PDB id
1pvb

 

 

 

 

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Contents
Protein chain
108 a.a. *
Ligands
NH4
Metals
_CA ×2
Waters ×72
* Residue conservation analysis
PDB id:
1pvb
Name: Calcium binding protein
Title: X-ray structure of a new crystal form of pike 4.10 parvalbumin
Structure: Parvalbumin. Chain: a. Engineered: yes
Source: Esox lucius. Northern pike. Organism_taxid: 8010
Resolution:
1.75Å     R-factor:   0.168    
Authors: J.P.Declercq,B.Tinant,J.Parello
Key ref:
J.P.Declercq et al. (1996). X-ray structure of a new crystal form of pike 4.10 beta parvalbumin. Acta Crystallogr D Biol Crystallogr, 52, 165-169. PubMed id: 15299738 DOI: 10.1107/S0907444995010006
Date:
05-Jan-95     Release date:   27-Feb-95    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P02619  (PRVB_ESOLU) -  Parvalbumin beta from Esox lucius
Seq:
Struc:
107 a.a.
107 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1107/S0907444995010006 Acta Crystallogr D Biol Crystallogr 52:165-169 (1996)
PubMed id: 15299738  
 
 
X-ray structure of a new crystal form of pike 4.10 beta parvalbumin.
J.P.Declercq, B.Tinant, J.Parello.
 
  ABSTRACT  
 
A new crystal form of pike (pI 4.10) parvalbumin has been crystallized in presence of EDTA at pH 8.0. The crystals are orthorhombic, space group P2(1)2(1)2(1), with a = 51.84, b = 49.95, c = 34.96 A. Diffractometer data were collected to 1.75 A. The structure was solved by molecular replacement and in the range 8.0-1.75 A. In spite of the presence of EDTA, calcium ions are present in both primary binding sites. As compared to the previously reported structures, the main differences concern the conformation of the N-terminal residues and the packing in the unit cell.
 
  Selected figure(s)  
 
Figure 5.
Fig. 5. Superposition of the Ca atoms of pike (p/4.10) parvalbumin crystallized in the presence of EDTA (this study, thick lines) and in the absence of EDTA [1PAL, Declercq et al. (1991), thin lines].
Figure 5.
Fig. 5. Superposition of the Ca atoms of pike (p/4.10) parvalbumin crystallized in the presence of EDTA (this study, thick lines) and in the absence of EDTA [1PAL, Declercq et al. (1991), thin lines].
 
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1996, 52, 165-169) copyright 1996.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
18260106 S.E.Permyakov, A.G.Bakunts, A.I.Denesyuk, E.L.Knyazeva, V.N.Uversky, and E.A.Permyakov (2008).
Apo-parvalbumin as an intrinsically disordered protein.
  Proteins, 72, 822-836.  
10233057 J.M.Zanotti, M.C.Bellissent-Funel, and J.Parello (1999).
Hydration-coupled dynamics in proteins studied by neutron scattering and NMR: the case of the typical EF-hand calcium-binding parvalbumin.
  Biophys J, 76, 2390-2411.  
  10548066 J.P.Declercq, C.Evrard, V.Lamzin, and J.Parello (1999).
Crystal structure of the EF-hand parvalbumin at atomic resolution (0.91 A) and at low temperature (100 K). Evidence for conformational multistates within the hydrophobic core.
  Protein Sci, 8, 2194-2204.
PDB code: 2pvb
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 code is shown on the right.

 

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