spacer
spacer

PDBsum entry 3v98

Go to PDB code: 
protein metals Protein-protein interface(s) links
Oxidoreductase PDB id
3v98

 

 

 

 

Loading ...

 
JSmol PyMol  
Contents
Protein chain
669 a.a.
Metals
FE2 ×2
Waters ×956
PDB id:
3v98
Name: Oxidoreductase
Title: S663d stable-5-lox
Structure: Arachidonate 5-lipoxygenase. Chain: a, b. Synonym: 5-lo, 5-lipoxygenase. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: alox5, log5. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.07Å     R-factor:   0.167     R-free:   0.197
Authors: N.C.Gilbert,Z.Rui,D.B.Neau,M.Waight,S.G.Bartlett,W.E.Boeglin, A.R.Brash,M.E.Newcomer
Key ref: N.C.Gilbert et al. (2012). Conversion of human 5-lipoxygenase to a 15-lipoxygenase by a point mutation to mimic phosphorylation at Serine-663. Faseb J, 26, 3222-3229. PubMed id: 22516296
Date:
23-Dec-11     Release date:   02-May-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P09917  (LOX5_HUMAN) -  Polyunsaturated fatty acid 5-lipoxygenase from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
674 a.a.
669 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 12 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 2: E.C.1.13.11.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 3: E.C.1.13.11.34  - arachidonate 5-lipoxygenase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
      Reaction: (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = leukotriene A4 + H2O
(5Z,8Z,11Z,14Z)-eicosatetraenoate
+ O2
= leukotriene A4
+ H2O
      Cofactor: Fe cation
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    
 
 
Faseb J 26:3222-3229 (2012)
PubMed id: 22516296  
 
 
Conversion of human 5-lipoxygenase to a 15-lipoxygenase by a point mutation to mimic phosphorylation at Serine-663.
N.C.Gilbert, Z.Rui, D.B.Neau, M.T.Waight, S.G.Bartlett, W.E.Boeglin, A.R.Brash, M.E.Newcomer.
 
  ABSTRACT  
 
No abstract given.

 

 

spacer

spacer