PDBsum entry: 1asg

Aminotransferase

PDB id: 1asg

Contents

Protein chain

396 a.a. *

Ligands

PLP

MAE

Waters ×135

* Residue conservation analysis

PDB id:

1asg

Name:

Aminotransferase

Title:

The structural basis for the reduced activity of the y226f(y active site mutant of e. Coli aspartate aminotransferase

Structure:

Aspartate aminotransferase. Chain: a. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562

Biol. unit:

Dimer (from PQS)

Resolution:

2.80Å R-factor: 0.200

Authors:

C.Schumacher,D.Ringe

Key ref:

C.Schumacher and d.ringe The structural basis for the reduced activity of the y226f(y225f) active site mutant of e. Coli aspartate aminotransferase. To be published,

Date:

27-Aug-93 Release date: 30-Apr-94

Protein chain

P00509  (AAT_ECOLI) -  Aspartate aminotransferase

Seq: 396 a.a.

Struc: 396 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.2.6.1.1 - Aspartate transaminase.
• Reaction: L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate

L-aspartate (Bound ligand (Het Group name = MAE) matches with 88.89% similarity) + 2-oxoglutarate = oxaloacetate + L-glutamate

• Cofactor: Pyridoxal 5'-phosphate

Pyridoxal 5'-phosphate (Bound ligand (Het Group name = PLP) matches with 93.75% similarity)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Cellular component: cytoplasm (2 terms)
• Biological process: biosynthetic process (4 terms)
• Biochemical function: catalytic activity (10 terms)