Structure of PDB 12as Chain B

Receptor sequence
>12asB (length=327) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
AYIAKQRQISFVKSHFSRQLEERLGLIEVQAPILSRVGDGTQDNLSGAEK
AVQVKVKALPDAQFEVVHSLAKWKRQTLGQHDFSAGEGLYTHMKALRPDE
DRLSPLHSVYVDQWDWERVMGDGERQFSTLKSTVEAIWAGIKATEAAVSE
EFGLAPFLPDQIHFVHSQELLSRYPDLDAKGRERAIAKDLGAVFLVGIGG
KLSDGHRHDVRAPDYDDWSTPSELGHAGLNGDILVWNPVLEDAFELSSMG
IRVDADTLKHQLALTGDEDRLELEWHQALLRGEMPQTIGGGIGQSRLTML
LLQLPHIGQVQAGVWPAAVRESVPSLL
3D structure
PDB12as Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl-tRNA synthetase.
ChainB
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 B S72 A74 K77 Q116 D118 Y218 S251 R255 G293 S69 A71 K74 Q113 D115 Y215 S248 R252 G290
BS02 AMP B R100 E103 S111 V114 Q116 E248 L249 S250 S251 G296 R299 R97 E100 S108 V111 Q113 E245 L246 S247 S248 G293 R296
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

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Biological Process
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Cellular Component
External links
PDB RCSB:12as, PDBe:12as, PDBj:12as
PDBsum12as
PubMed9437423
UniProtP00963|ASNA_ECOLI Aspartate--ammonia ligase (Gene Name=asnA)

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