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PDBsum entry 2wz1

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protein ligands Protein-protein interface(s) links
Lyase PDB id
2wz1
Jmol
Contents
Protein chain
197 a.a. *
Ligands
EDO ×3
Waters ×289
* Residue conservation analysis
PDB id:
2wz1
Name: Lyase
Title: Structure of the catalytic domain of human soluble guanylate cyclase 1 beta 3.
Structure: Guanylate cyclase soluble subunit beta-1. Chain: a, b. Fragment: catalytic domain, residues 994-1205. Synonym: guanylate cyclase 1 beta 3, gcs-beta-1, soluble gu cyclase small subunit, gcs-beta-3. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: r3 prare2.
Resolution:
1.63Å     R-factor:   0.185     R-free:   0.219
Authors: C.K.Allerston,C.D.O.Cooper,J.Muniz,A.C.W.Pike,F.Von Delft, C.H.Arrowsmith,J.Weigelt,A.Edwards,C.Bountra,O.Gileadi
Key ref: C.K.Allerston et al. (2013). Crystal structures of the catalytic domain of human soluble guanylate cyclase. PLoS One, 8, e57644. PubMed id: 23505436 DOI: 10.1371/journal.pone.0057644
Date:
23-Nov-09     Release date:   01-Dec-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q02153  (GCYB1_HUMAN) -  Guanylate cyclase soluble subunit beta-1
Seq:
Struc:
 
Seq:
Struc:
619 a.a.
197 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.4.6.1.2  - Guanylate cyclase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: GTP = 3',5'-cyclic GMP + diphosphate
GTP
= 3',5'-cyclic GMP
+ diphosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     intracellular signal transduction   2 terms 
  Biochemical function     phosphorus-oxygen lyase activity     1 term  

 

 
    reference    
 
 
DOI no: 10.1371/journal.pone.0057644 PLoS One 8:e57644 (2013)
PubMed id: 23505436  
 
 
Crystal structures of the catalytic domain of human soluble guanylate cyclase.
C.K.Allerston, F.von Delft, O.Gileadi.
 
  ABSTRACT  
 
No abstract given.