Structure of PDB 3rex Chain A

Receptor sequence
>3rexA (length=294) Species: 29292 (Pyrococcus abyssi) [Search protein sequence]
MNAVEIISRDIYKAIDIQTKILDYMTKFFTDRGFKWLLPIMLSPITDPLW
PDPAGEGIRPAEVDVYGVRMRLTHSMILHKQLAIAMGLEKIFVLSPNIRL
ESRRKDDGRHSYEFTQLDFEIEGAKMKDVMRLIEELIYGLFRKAEEWTGR
EFPRARHFKVYDYKDILEEFGSDEKASMEMEEPFWIVNIPREFYDREENG
VWKNYDLILPYGYGEVSSGGEREWEYEKIVAKIRAAGLKEDSFRPYLEIA
RAGKLKPSAGAGIGVERLVRFIVGAKHIAEVQPFPRVPGIPAVI
3D structure
PDB3rex Crystal Structure of the Archaeal Asparagine Synthetase: Interrelation with Aspartyl-tRNA and Asparaginyl-tRNA Synthetases.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 AMP A R99 H110 S111 F114 Q116 E215 V216 S217 G264 R267 R99 H110 S111 F114 Q116 E215 V216 S217 G264 R267
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3rex, PDBe:3rex, PDBj:3rex
PDBsum3rex
PubMed21820443
UniProtQ9V228

[Back to BioLiP]