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PDBsum entry 2lhi

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protein metals links
Metal binding protein PDB id
2lhi

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
176 a.a.
Metals
_CA ×3
PDB id:
2lhi
Name: Metal binding protein
Title: Solution structure of ca2+/cna1 peptide-bound ycam
Structure: Calmodulin,serine/threonine-protein phosphatase 2b catalytic subunit a1. Chain: a. Synonym: cam,calcineurin a1,calmodulin-binding protein 1. Engineered: yes. Other_details: the fusion protein of calmodulin (residue 1-146), linker (gsstg) and calcineurin a1 (residues 453-476)
Source: Saccharomyces cerevisiae (strain atcc 204508 / s288c). Baker's yeast. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Gene: cmd1, ybr109c, ybr0904, cmp1, cna1, l9753.6, ylr433c. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 20 models
Authors: K.Ogura,K.Takahashi,Y.Kobashigawa,R.Yoshida,H.Itoh,M.Yazawa,F.Inagaki
Key ref: K.Ogura et al. (2012). Solution structures of yeast Saccharomyces cerevisiae calmodulin in calcium- and target peptide-bound states reveal similarities and differences to vertebrate calmodulin. Genes Cells, 17, 159-172. PubMed id: 22280008
Date:
10-Aug-11     Release date:   29-Aug-12    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P06787  (CALM_YEAST) -  Calmodulin from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
147 a.a.
176 a.a.*
Protein chain
Pfam   ArchSchema ?
P23287  (PP2B1_YEAST) -  Serine/threonine-protein phosphatase 2B catalytic subunit A1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
 
Seq:
Struc:
553 a.a.
176 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 146 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 2: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 3: E.C.3.1.3.16  - protein-serine/threonine phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction:
1. O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] + phosphate
2. O-phospho-L-threonyl-[protein] + H2O = L-threonyl-[protein] + phosphate
O-phospho-L-seryl-[protein]
+ H2O
= L-seryl-[protein]
+ phosphate
O-phospho-L-threonyl-[protein]
+ H2O
= L-threonyl-[protein]
+ phosphate
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
Genes Cells 17:159-172 (2012)
PubMed id: 22280008  
 
 
Solution structures of yeast Saccharomyces cerevisiae calmodulin in calcium- and target peptide-bound states reveal similarities and differences to vertebrate calmodulin.
K.Ogura, H.Kumeta, K.Takahasi, Y.Kobashigawa, R.Yoshida, H.Itoh, M.Yazawa, F.Inagaki.
 
  ABSTRACT  
 
No abstract given.

 

 

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