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PDBsum entry 3nmd

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protein ligands Protein-protein interface(s) links
Transferase PDB id
3nmd

 

 

 

 

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Contents
Protein chains
53 a.a.
47 a.a.
53 a.a.
50 a.a.
Ligands
HEZ ×7
GOL
Waters ×100
PDB id:
3nmd
Name: Transferase
Title: Crystal structure of the leucine zipper domain of cgmp dependent protein kinase i beta
Structure: Cgmp dependent protein kinase. Chain: a, b, c, d, e. Fragment: dimerization docking domain, unp residues 4-55. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: prkg1. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Resolution:
2.27Å     R-factor:   0.197     R-free:   0.248
Authors: C.Kim,D.E.Casteel,E.V.Smith-Nguyen,B.Sankaran,Berkeley Structural Genomics Center (Bsgc)
Key ref: D.E.Casteel et al. (2010). A crystal structure of the cyclic GMP-dependent protein kinase I{beta} dimerization/docking domain reveals molecular details of isoform-specific anchoring. J Biol Chem, 285, 32684-32688. PubMed id: 20826808
Date:
22-Jun-10     Release date:   08-Sep-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q13976  (KGP1_HUMAN) -  cGMP-dependent protein kinase 1 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
671 a.a.
53 a.a.*
Protein chain
Pfam   ArchSchema ?
Q13976  (KGP1_HUMAN) -  cGMP-dependent protein kinase 1 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
671 a.a.
47 a.a.*
Protein chain
Pfam   ArchSchema ?
Q13976  (KGP1_HUMAN) -  cGMP-dependent protein kinase 1 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
671 a.a.
53 a.a.*
Protein chains
Pfam   ArchSchema ?
Q13976  (KGP1_HUMAN) -  cGMP-dependent protein kinase 1 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
671 a.a.
50 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 127 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains A, B, C, D, E: E.C.2.7.11.12  - cGMP-dependent protein kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction:
1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H+
L-seryl-[protein]
+ ATP
= O-phospho-L-seryl-[protein]
+ ADP
+ H(+)
L-threonyl-[protein]
+ ATP
= O-phospho-L-threonyl-[protein]
+ ADP
+ H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
J Biol Chem 285:32684-32688 (2010)
PubMed id: 20826808  
 
 
A crystal structure of the cyclic GMP-dependent protein kinase I{beta} dimerization/docking domain reveals molecular details of isoform-specific anchoring.
D.E.Casteel, E.V.Smith-Nguyen, B.Sankaran, S.H.Roh, R.B.Pilz, C.Kim.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
  21517872 J.C.Harris, M.Hrmova, S.Lopato, and P.Langridge (2011).
Modulation of plant growth by HD-Zip class I and II transcription factors in response to environmental stimuli.
  New Phytol, 190, 823-837.  
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.

 

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