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PDBsum entry 2ll6

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protein Protein-protein interface(s) links
Oxidoreductase PDB id
2ll6

 

 

 

 

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Contents
Protein chains
148 a.a.
17 a.a.
PDB id:
2ll6
Name: Oxidoreductase
Title: Solution nmr structure of cam bound to inos cam binding domain peptide
Structure: Calmodulin. Chain: a. Synonym: cam. Engineered: yes. Nitric oxide synthase, inducible. Chain: b. Fragment: calmodulin-binding region residues 515-531. Synonym: hepatocyte nos, hep-nos, inducible no synthase, inducible nos, inos, nos type ii, peptidyl-cysteine s-nitrosylase nos2.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: calm1, calm, cam, cam1, calm2, cam2, camb, calm3, calml2, cam3, camc, camiii. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: nos2, nos2a.
NMR struc: 20 models
Authors: M.Piazza,K.Futrega,D.E.Spratt,T.Dieckmann,J.G.Guillemette
Key ref: M.Piazza et al. (2012). Structure and dynamics of calmodulin (CaM) bound to nitric oxide synthase peptides: effects of a phosphomimetic CaM mutation. Biochemistry, 51, 3651-3661. PubMed id: 22486744
Date:
29-Oct-11     Release date:   16-May-12    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P0DP23  (CALM1_HUMAN) -  Calmodulin-1 from Homo sapiens
Seq:
Struc:
149 a.a.
148 a.a.
Protein chain
Pfam   ArchSchema ?
P35228  (NOS2_HUMAN) -  Nitric oxide synthase, inducible from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1153 a.a.
17 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class: Chain B: E.C.1.14.13.39  - nitric-oxide synthase (NADPH).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 2 L-arginine + 3 NADPH + 4 O2 + H+ = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
2 × L-arginine
+ 3 × NADPH
+ 4 × O2
+ H(+)
= 2 × L-citrulline
+ 2 × nitric oxide
+ 3 × NADP(+)
+ 4 × H2O
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Biochemistry 51:3651-3661 (2012)
PubMed id: 22486744  
 
 
Structure and dynamics of calmodulin (CaM) bound to nitric oxide synthase peptides: effects of a phosphomimetic CaM mutation.
M.Piazza, K.Futrega, D.E.Spratt, T.Dieckmann, J.G.Guillemette.
 
  ABSTRACT  
 
No abstract given.

 

 

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