Structure of PDB 11as Chain A

Receptor sequence

>11asA (length=327) Species: 83333 (Escherichia coli K-12)

AYIAKQRQISFVKSHFSRQLEERLGLIEVQAPILSRVGDGTQDNLSGAEK
AVQVKVKALPDAQFEVVHSLAKWKRQTLGQHDFSAGEGLYTHMKALRPDE
DRLSPLHSVYVDQWDWERVMGDGERQFSTLKSTVEAIWAGIKATEAAVSE
EFGLAPFLPDQIHFVHSQELLSRYPDLDAKGRERAIAKDLGAVFLVGIGG
KLSDGHRHDVRAPDYDDWSTPSELGHAGLNGDILVWNPVLEDAFELSSMG
IRVDADTLKHQLALTGDEDRLELEWHQALLRGEMPQTIGGGIGQSRLTML
LLQLPHIGQVQAGVWPAAVRESVPSLL

3D structure

• PDB: 11as Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl-tRNA synthetase.
• Chain: A
• Resolution: 2.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D46 R100 Q116 D235 E248 S251
• Catalytic site (residue number reindexed from 1): D43 R97 Q113 D232 E245 S248
• Enzyme Commision number: 6.3.1.1: aspartate--ammonia ligase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	ASN	A	D46 A74 Q116 Y218 S251 R255	D43 A71 Q113 Y215 S248 R252

Gene Ontology

Molecular Function

• GO:0004071 aspartate-ammonia ligase activity
• GO:0005524 ATP binding
• GO:0016874 ligase activity
• GO:0042802 identical protein binding
• GO:0042803 protein homodimerization activity

Biological Process

• GO:0006529 asparagine biosynthetic process
• GO:0006974 DNA damage response
• GO:0070981 L-asparagine biosynthetic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:11as, PDBe:11as, PDBj:11as
• PDBsum: 11as
• PubMed: 9437423
• UniProt: P00963|ASNA_ECOLI Aspartate--ammonia ligase (Gene Name=asnA)