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PDBsum entry 4ae6

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protein ligands Protein-protein interface(s) links
Transferase PDB id
4ae6

 

 

 

 

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Contents
Protein chain
321 a.a.
Ligands
ACT
Waters ×255
PDB id:
4ae6
Name: Transferase
Title: Structure and function of the human sperm-specific isoform of protein kinase a (pka) catalytic subunit calpha 2
Structure: Camp-dependent protein kinase catalytic subunit alpha 2. Chain: a, b. Synonym: pka c-alpha, pka c-alpha 2. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Cell: spermatozoa. Expressed in: escherichia coli. Expression_system_taxid: 511693. Expression_system_variant: rosetta plyss.
Resolution:
2.10Å     R-factor:   0.219     R-free:   0.283
Authors: T.H.Hereng,P.H.Backe,J.Kahmann,C.Scheich,M.Bjoras,B.S.Skalhegg, K.R.Rosendal
Key ref: T.H.Hereng et al. (2012). Structure and function of the human sperm-specific isoform of protein kinase A (PKA) catalytic subunit Cα2. J Struct Biol, 178, 300-310. PubMed id: 22504716
Date:
09-Jan-12     Release date:   18-Apr-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P17612  (KAPCA_HUMAN) -  cAMP-dependent protein kinase catalytic subunit alpha from Homo sapiens
Seq:
Struc:
351 a.a.
321 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.2.7.11.11  - cAMP-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 Struct Biol 178:300-310 (2012)
PubMed id: 22504716  
 
 
Structure and function of the human sperm-specific isoform of protein kinase A (PKA) catalytic subunit Cα2.
T.H.Hereng, P.H.Backe, J.Kahmann, C.Scheich, M.Bjørås, B.S.Skålhegg, K.R.Rosendal.
 
  ABSTRACT  
 
No abstract given.

 

 

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