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PDBsum entry 7rdf

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protein ligands links
Flavoprotein PDB id
7rdf

 

 

 

 

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Contents
Protein chain
375 a.a.
Ligands
4R2-6FA
GOL ×3
PEG
Waters ×432
PDB id:
7rdf
Name: Flavoprotein
Title: Crystal structure of pseudomonas aeruginosa d-arginine dehydrogenase y249f co-crystallized in the presence of d-arginine
Structure: Fad-dependent catabolic d-arginine dehydrogenase daua. Chain: a. Synonym: d-arginine dehydrogenase,dadh,d-arginine utilization protein a,dau. Engineered: yes
Source: Pseudomonas aeruginosa (strain atcc 15692 / dsm 22644 / cip 104116 / jcm 14847 / lmg 12228 / 1c / prs 101 / pao1). Organism_taxid: 208964. Strain: atcc 15692 / dsm 22644 / cip 104116 / jcm 14847 / lmg 12228 / 1c / prs 101 / pao1. Atcc: 15692. Gene: daua, pa3863. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.29Å     R-factor:   0.128     R-free:   0.157
Authors: R.A.G.Reis,A.Iyer,A.Agniswamy,I.T.Weber,G.Gadda
Key ref: A.Iyer et al. (2021). Discovery of a new flavin n5-Adduct in a tyrosine to phenylalanine variant of d-Arginine dehydrogenase.. Arch.Biochem.Biophys., 715, 09100. PubMed id: 34864048 DOI: 10.1016/J.ABB.2021.109100
Date:
09-Jul-21     Release date:   22-Dec-21    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9HXE3  (DAUA_PSEAE) -  FAD-dependent catabolic D-arginine dehydrogenase DauA from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Seq:
Struc:
375 a.a.
375 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.1.4.99.6  - D-arginine dehydrogenase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: D-arginine + A + H2O = 5-guanidino-2-oxopentanoate + AH2 + NH4+
D-arginine
+
+ H2O
= 5-guanidino-2-oxopentanoate
+ AH2
+ NH4(+)
      Cofactor: FAD
FAD
Bound ligand (Het Group name = 4R2) matches with 85.48% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 

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