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PDBsum entry 2ax2

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protein metals links
Lyase PDB id
2ax2
Jmol
Contents
Protein chain
258 a.a. *
Metals
_ZN
Waters ×218
* Residue conservation analysis
PDB id:
2ax2
Name: Lyase
Title: Production and x-ray crystallographic analysis of fully deuterated human carbonic anhydrase ii
Structure: Carbonic anhydrase ii. Chain: a. Synonym: carbonate dehydratase ii, ca-ii, carbonic anhydrasE C. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ca2. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
Resolution:
1.50Å     R-factor:   0.195     R-free:   0.206
Authors: M.Budayova-Spano,S.Z.Fisher,M.T.Dauvergne,D.N.Silverman, D.A.A.Myles,R.M.Mckenna
Key ref:
M.Budayova-Spano et al. (2006). Production and X-ray crystallographic analysis of fully deuterated human carbonic anhydrase II. Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 6-9. PubMed id: 16511248 DOI: 10.1107/S1744309105038248
Date:
02-Sep-05     Release date:   03-Jan-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00918  (CAH2_HUMAN) -  Carbonic anhydrase 2
Seq:
Struc:
260 a.a.
258 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.4.2.1.1  - Carbonate dehydratase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: H2CO3 = CO2 + H2O
H(2)CO(3)
= CO(2)
+ H(2)O
      Cofactor: Zn(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular space   11 terms 
  Biological process     angiotensin-mediated signaling pathway   22 terms 
  Biochemical function     protein binding     5 terms  

 

 
    Added reference    
 
 
DOI no: 10.1107/S1744309105038248 Acta Crystallogr Sect F Struct Biol Cryst Commun 62:6-9 (2006)
PubMed id: 16511248  
 
 
Production and X-ray crystallographic analysis of fully deuterated human carbonic anhydrase II.
M.Budayova-Spano, S.Z.Fisher, M.T.Dauvergne, M.Agbandje-McKenna, D.N.Silverman, D.A.Myles, R.McKenna.
 
  ABSTRACT  
 
Human carbonic anhydrase II (HCA II) is a zinc metalloenzyme that catalyzes the reversible hydration and dehydration of carbon dioxide and bicarbonate, respectively. The rate-limiting step in catalysis is the intramolecular transfer of a proton between the zinc-bound solvent (H2O/OH-) and the proton-shuttling residue His64. This distance (approximately 7.5 A) is spanned by a well defined active-site solvent network stabilized by amino-acid side chains (Tyr7, Asn62, Asn67, Thr199 and Thr200). Despite the availability of high-resolution (approximately 1.0 A) X-ray crystal structures of HCA II, there is currently no definitive information available on the positions and orientations of the H atoms of the solvent network or active-site amino acids and their ionization states. In preparation for neutron diffraction studies to elucidate this hydrogen-bonding network, perdeuterated HCA II has been expressed, purified, crystallized and its X-ray structure determined to 1.5 A resolution. The refined structure is highly isomorphous with hydrogenated HCA II, especially with regard to the active-site architecture and solvent network. This work demonstrates the suitability of these crystals for neutron macromolecular crystallography.
 
  Selected figure(s)  
 
Figure 1.
Active site of (a) hydrogenated and (b) perdeuterated HCA II. Important catalytic side chains in the active sites are shown in yellow ball-and-stick representation and are as labeled. The Zn atom is shown as a black sphere, while solvent molecules are in red. Inferred hydrogen bonds are shown as orange dashed lines. (a) Hydrogenated HCA II (PDB code 1tbt; Fisher et al., 2005[triangle]) and (b) perdeuterated HCA II; the blue electron density shown is a 2F [o] [minus sign] F [c] map contoured at 1.5[sigma]. The figure was generated and rendered using MOLSCRIPT and RASTER3D (Esnouf, 1999[triangle]; Merritt & Bacon, 1997[triangle]). Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 January 1; 62(Pt 1): 6–9. Published online 2005 December 16. doi: 10.1107/S1744309105038248. Copyright [copyright] International Union of Crystallography 2006
Figure 2.
Optical photograph of a perdeuterated HCA II crystal of approximate dimensions 0.4 x 0.4 x 0.1 mm. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 January 1; 62(Pt 1): 6–9. Published online 2005 December 16. doi: 10.1107/S1744309105038248. Copyright [copyright] International Union of Crystallography 2006
 
  The above figures are reprinted from an Open Access publication published by the IUCr: Acta Crystallogr Sect F Struct Biol Cryst Commun (2006, 62, 6-9) copyright 2006.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
  20383004 M.M.Blum, S.J.Tomanicek, H.John, B.L.Hanson, H.Rüterjans, B.P.Schoenborn, P.Langan, and J.C.Chen (2010).
X-ray structure of perdeuterated diisopropyl fluorophosphatase (DFPase): perdeuteration of proteins for neutron diffraction.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 66, 379-385.
PDB code: 3kgg
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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