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PDBsum entry 4xdu

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protein ligands metals links
Transferase PDB id
4xdu

 

 

 

 

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Contents
Protein chain
330 a.a.
Ligands
ADP
EDO ×3
ACT ×2
Metals
_MG ×2
_NA ×2
Waters ×255
PDB id:
4xdu
Name: Transferase
Title: Crystal structure of treponema pallidum tp0796 flavin trafficking protein,a bifunctional fmn transferase/fad pyrophosphatase, n55y mutant, adp bound form
Structure: Fad:protein fmn transferase. Chain: a. Synonym: flavin transferase. Engineered: yes. Mutation: yes
Source: Treponema pallidum (strain nichols). Organism_taxid: 243276. Strain: nichols. Gene: apbe, tp_0796. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.35Å     R-factor:   0.169     R-free:   0.188
Authors: D.R.Tomchick,C.A.Brautigam,R.K.Deka,M.V.Norgard
Key ref: R.K.Deka et al. (2015). Evidence for Posttranslational Protein Flavinylation in the Syphilis Spirochete Treponema pallidum: Structural and Biochemical Insights from the Catalytic Core of a Periplasmic Flavin-Trafficking Protein. Mbio, 6, e00519. PubMed id: 25944861 DOI: 10.1128/mBio.00519-15
Date:
20-Dec-14     Release date:   14-Oct-15    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
O83774  (APBE_TREPA) -  FAD:protein FMN transferase from Treponema pallidum (strain Nichols)
Seq:
Struc:
362 a.a.
330 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.2.7.1.180  - FAD:protein Fmn transferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-threonyl-[protein] + FAD = FMN-L-threonyl-[protein] + AMP + H+
L-threonyl-[protein]
+ FAD
= FMN-L-threonyl-[protein]
Bound ligand (Het Group name = ADP)
matches with 85.19% similarity
+ AMP
+ H(+)
      Cofactor: Mg(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
DOI no: 10.1128/mBio.00519-15 Mbio 6:e00519 (2015)
PubMed id: 25944861  
 
 
Evidence for Posttranslational Protein Flavinylation in the Syphilis Spirochete Treponema pallidum: Structural and Biochemical Insights from the Catalytic Core of a Periplasmic Flavin-Trafficking Protein.
R.K.Deka, C.A.Brautigam, W.Z.Liu, D.R.Tomchick, M.V.Norgard.
 
  ABSTRACT  
 
No abstract given.

 

 

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