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PDBsum entry 3v3h

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protein metals links
Lyase PDB id
3v3h

 

 

 

 

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Contents
Protein chain
258 a.a.
Metals
_CL
_ZN
Waters ×220
PDB id:
3v3h
Name: Lyase
Title: Kinetic and structural studies of thermostabilized mutants of hca ii.
Structure: Carbonic anhydrase 2. Chain: b. Synonym: carbonate dehydratase ii, carbonic anhydrasE C, cac, carbonic anhydrase ii, ca-ii. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ca2. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.85Å     R-factor:   0.168     R-free:   0.224
Authors: C.D.Boone,S.Z.Fisher,R.Mckenna
Key ref: Z.Fisher et al. (2012). Kinetic and structural characterization of thermostabilized mutants of human carbonic anhydrase II. Protein Eng Des Sel, 25, 347-355. PubMed id: 22691706
Date:
13-Dec-11     Release date:   20-Jun-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
P00918  (CAH2_HUMAN) -  Carbonic anhydrase 2 from Homo sapiens
Seq:
Struc:
260 a.a.
258 a.a.*
Key:    Secondary structure  CATH domain
* PDB and UniProt seqs differ at 5 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 2: E.C.4.2.1.1  - carbonic anhydrase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: hydrogencarbonate + H+ = CO2 + H2O
hydrogencarbonate
+ H(+)
= CO2
+ H2O
      Cofactor: Zn(2+)
   Enzyme class 3: E.C.4.2.1.69  - cyanamide hydratase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: urea = cyanamide + H2O
urea
= cyanamide
+ H2O
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Protein Eng Des Sel 25:347-355 (2012)
PubMed id: 22691706  
 
 
Kinetic and structural characterization of thermostabilized mutants of human carbonic anhydrase II.
Z.Fisher, C.D.Boone, S.M.Biswas, B.Venkatakrishnan, M.Aggarwal, C.Tu, M.Agbandje-McKenna, D.Silverman, R.McKenna.
 
  ABSTRACT  
 
No abstract given.

 

 

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