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PDBsum entry 1cnj

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protein metals links
Lyase (oxo-acid) PDB id
1cnj
Jmol PyMol
Contents
Protein chain
257 a.a. *
Metals
_HG
_ZN
Waters ×203
* Residue conservation analysis
PDB id:
1cnj
Name: Lyase (oxo-acid)
Title: X-ray crystallographic studies of engineered hydrogen bond networks in a protein-zinc binding site
Structure: Carbonic anhydrase ii. Chain: a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ca2.
Resolution:
1.80Å     R-factor:   0.169    
Authors: C.A.Lesburg,D.W.Christianson
Key ref: C.A.Lesburg and d.w.christianson (1995). X-Ray crystallographic studies of engineered hydrogen bond networks in a protein-Zinc binding site. J.Am.Chem.Soc., 117, 6838-6844.
Date:
03-Apr-95     Release date:   10-Jul-95    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00918  (CAH2_HUMAN) -  Carbonic anhydrase 2
Seq:
Struc:
260 a.a.
257 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.4.2.1.1  - Carbonic anhydrase.
[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     6 terms  

 

 

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