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PDBsum entry 1vra

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protein ligands Protein-protein interface(s) links
Transferase PDB id
1vra
Jmol
Contents
Protein chains
191 a.a. *
213 a.a. *
Ligands
SO4 ×2
UNL
EDO ×16
Waters ×390
* Residue conservation analysis
PDB id:
1vra
Name: Transferase
Title: Crystal structure of arginine biosynthesis bifunctional prot (10175521) from bacillus halodurans at 2.00 a resolution
Structure: Arginine biosynthesis bifunctional protein argj. Chain: a. Fragment: alpha chain, residues 1-196. Engineered: yes. Arginine biosynthesis bifunctional protein argj. Chain: b. Fragment: beta chain, residues 197-411. Engineered: yes
Source: Bacillus halodurans. Organism_taxid: 86665. Gene: argj. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: both chain a and chain b were expressed from construct which encodes residues 1-411 of the argj gene. Construct which encodes residues 1-411 of the argj gene
Biol. unit: Dimer (from PQS)
Resolution:
2.00Å     R-factor:   0.141     R-free:   0.158
Authors: Joint Center For Structural Genomics (Jcsg)
Key ref: Joint center for structural genomics (jcsg) Crystal structure of arginine biosynthesis bifunctional protein argj (10175521) from bacillus halodurans at 2.00 a resolution. To be published, .
Date:
17-Feb-05     Release date:   12-Apr-05    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9K8V3  (ARGJ_BACHD) -  Arginine biosynthesis bifunctional protein ArgJ
Seq:
Struc:
411 a.a.
191 a.a.
Protein chain
Pfam   ArchSchema ?
Q9K8V3  (ARGJ_BACHD) -  Arginine biosynthesis bifunctional protein ArgJ
Seq:
Struc:
411 a.a.
213 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class 1: Chains A, B: E.C.2.3.1.1  - Amino-acid N-acetyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Ornithine Biosynthesis
      Reaction: Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate
Acetyl-CoA
+ L-glutamate
= CoA
+ N-acetyl-L-glutamate
   Enzyme class 2: Chains A, B: E.C.2.3.1.35  - Glutamate N-acetyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: N2-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L- glutamate
N(2)-acetyl-L-ornithine
+ L-glutamate
= L-ornithine
+ N-acetyl-L- glutamate
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
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     arginine biosynthetic process   1 term 
  Biochemical function     glutamate N-acetyltransferase activity     1 term