PDBsum entry 3mwo

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protein metals Protein-protein interface(s) links
Lyase PDB id
Protein chain
257 a.a. *
_ZN ×2
Waters ×745
* Residue conservation analysis
PDB id:
Name: Lyase
Title: Human carbonic anhydrase ii in a doubled monoclinic cell: a determination
Structure: Carbonic anhydrase 2. Chain: a, b. Synonym: carbonic anhydrase ii, ca-ii, carbonate dehydratas carbonic anhydrasE C, cac. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ca2, hca2. Expressed in: escherichia coli. Expression_system_taxid: 562.
1.40Å     R-factor:   0.167     R-free:   0.184
Authors: A.H.Robbins,R.Mckenna
Key ref: A.H.Robbins et al. (2010). Structure of a monoclinic polymorph of human carbonic anhydrase II with a doubled a axis. Acta Crystallogr D Biol Crystallogr, 66, 628-634. PubMed id: 20445238
06-May-10     Release date:   09-Jun-10    
Supersedes: 3ks1
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P00918  (CAH2_HUMAN) -  Carbonic anhydrase 2
260 a.a.
257 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 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  


Acta Crystallogr D Biol Crystallogr 66:628-634 (2010)
PubMed id: 20445238  
Structure of a monoclinic polymorph of human carbonic anhydrase II with a doubled a axis.
A.H.Robbins, J.F.Domsic, M.Agbandje-McKenna, R.McKenna.
The crystal structure of human carbonic anhydrase II with a doubled a axis from that of the usually observed monoclinic unit cell has been determined and refined to 1.4 A resolution. The diffraction data with h = 2n + 1 were systematically weaker than those with h = 2n. Consequently, the scaling of the data, structure solution and refinement were challenging. The two molecules comprising the asymmetric unit are related by a noncrystallographic translation of (1/2) along a, but one of the molecules has two alternate positions related by a rotation of approximately 2 degrees. This rotation axis is located near the edge of the central beta-sheet, causing a maximum distance disparity of 1.7 A between equivalent atoms on the diametrically opposite side of the molecule. The crystal-packing contacts are similar to two sequential combined unit cells along a of the previously determined monoclinic unit cell. Abnormally high final R(cryst) and R(free) values (20.2% and 23.7%, respectively) are not unusual for structures containing pseudo-translational symmetry and probably result from poor signal to noise in the weak h-odd data.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20693695 A.H.Robbins, J.F.Domsic, M.Agbandje-McKenna, and R.McKenna (2010).
Emerging from pseudo-symmetry: the redetermination of human carbonic anhydrase II in monoclinic P2(1) with a doubled a axis.
  Acta Crystallogr D Biol Crystallogr, 66, 950-952.
PDB code: 3mwo
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