Structure of PDB 3rl6 Chain A

Receptor sequence
>3rl6A (length=294) Species: 272844 (Pyrococcus abyssi GE5) [Search protein sequence]
MNAVEIISRDIYKAIDIQTKILDYMTKFFTDRGFKWLLPIMLSPITDPLW
PDPAGEGIRPAEVDVYGVRMRLTHSMILHKQLAIAMGLEKIFVLSPNIRL
ESRRKDDGRHSYEFTQLDFEIEGAKMKDVMRLIEELIYGLFRKAEEWTGR
EFPRARHFKVYDYKDILEEFGSDEKASMEMEEPFWIVNIPREFYDREENG
VWKNYDLILPYGYGEVSSGGEREWEYEKIVAKIRAAGLKEDSFRPYLEIA
RAGKLKPSAGAGIGVERLVRFIVGAKHIAEVQPFPRVPGIPAVI
3D structure
PDB3rl6 Crystal Structure of the Archaeal Asparagine Synthetase: Interrelation with Aspartyl-tRNA and Asparaginyl-tRNA Synthetases.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R99 E101 R109 H110
Catalytic site (residue number reindexed from 1) R99 E101 R109 H110
Enzyme Commision number ?
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 Q116 D118 S218 R222 A261 G262 Q116 D118 S218 R222 A261 G262
BS02 AMP A R99 H110 S111 F114 Q116 E215 V216 S217 G264 R267 R99 H110 S111 F114 Q116 E215 V216 S217 G264 R267
BS03 MG A E215 S218 E215 S218
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004816 asparagine-tRNA ligase activity
GO:0005524 ATP binding
GO:0046872 metal ion binding
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006421 asparaginyl-tRNA aminoacylation

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Molecular Function
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Biological Process
External links
PDB RCSB:3rl6, PDBe:3rl6, PDBj:3rl6
PDBsum3rl6
PubMed21820443
UniProtQ9V228

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