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PDBsum entry 3ar5

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protein ligands metals links
Hydrolase/hydrolase inhibitor PDB id
3ar5

 

 

 

 

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Contents
Protein chain
995 a.a. *
Ligands
TG1
TM1
PTY ×3
Metals
_NA
Waters ×212
* Residue conservation analysis
PDB id:
3ar5
Name: Hydrolase/hydrolase inhibitor
Title: Calcium pump crystal structure with bound tnp-amp and tg
Structure: Sarcoplasmic/endoplasmic reticulum calcium atpase 1. Chain: a. Synonym: serca1, sr ca(2+)-atpase 1, calcium pump 1, calcium- transporting atpase sarcoplasmic reticulum type, fast twitch skeletal muscle isoform, endoplasmic reticulum class 1/2 ca(2+) atpase. Ec: 3.6.3.8
Source: Oryctolagus cuniculus. Rabbits. Organism_taxid: 9986. Tissue: skeletal muscle (white)
Resolution:
2.20Å     R-factor:   0.262     R-free:   0.288
Authors: C.Toyoshima,S.Yonekura,J.Tsueda,S.Iwasawa
Key ref: C.Toyoshima et al. (2011). Trinitrophenyl derivatives bind differently from parent adenine nucleotides to Ca2+-ATPase in the absence of Ca2+. Proc Natl Acad Sci U S A, 108, 1833-1838. PubMed id: 21239683
Date:
24-Nov-10     Release date:   02-Feb-11    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P04191  (AT2A1_RABIT) -  Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 from Oryctolagus cuniculus
Seq:
Struc:
 
Seq:
Struc:
1001 a.a.
994 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.7.2.2.10  - P-type Ca(2+) transporter.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Ca2+(in) + ATP + H2O = Ca2+(out) + ADP + phosphate + H+
Ca(2+)(in)
+ ATP
+ H2O
= Ca(2+)(out)
Bound ligand (Het Group name = TM1)
matches with 54.76% similarity
+ ADP
+ phosphate
+ H(+)
      Cofactor: Mg(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Proc Natl Acad Sci U S A 108:1833-1838 (2011)
PubMed id: 21239683  
 
 
Trinitrophenyl derivatives bind differently from parent adenine nucleotides to Ca2+-ATPase in the absence of Ca2+.
C.Toyoshima, S.Yonekura, J.Tsueda, S.Iwasawa.
 
  ABSTRACT  
 
No abstract given.

 

 

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