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PDBsum entry 2e65

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protein Protein-protein interface(s) links
Ligase PDB id
2e65

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
227 a.a. *
Waters ×506
* Residue conservation analysis
PDB id:
2e65
Name: Ligase
Title: Crystal structure of biotin protein ligase from pyrococcus horikoshii ot3, mutation d104a
Structure: Biotin--[acetyl-coa-carboxylase] ligase. Chain: a, b. Synonym: biotin protein ligase. Engineered: yes. Mutation: yes
Source: Pyrococcus horikoshii. Organism_taxid: 53953. Gene: bpl. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.65Å     R-factor:   0.200     R-free:   0.224
Authors: B.Bagautdinov,N.Kunishima,Riken Structural Genomics/proteomics Initiative (Rsgi)
Key ref: B.Bagautdinov and n.kunishima Ligand structures of biotin protein ligase from pyrococcus horikoshii ot3. To be published, .
Date:
25-Dec-06     Release date:   26-Jun-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
O57883  (O57883_PYRHO) -  235aa long hypothetical biotin--[acetyl-CoA-carboxylase] ligase from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Seq:
Struc:
235 a.a.
227 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.6.3.4.15  - biotin--[biotin carboxyl-carrier protein] ligase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: biotin + L-lysyl-[protein] + ATP = N6-biotinyl-L-lysyl-[protein] + AMP + diphosphate + H+
biotin
+ L-lysyl-[protein]
+ ATP
= N(6)-biotinyl-L-lysyl-[protein]
+ AMP
+ diphosphate
+ H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

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