Structure of PDB 3rex Chain B

Receptor sequence
>3rexB (length=290) Species: 29292 (Pyrococcus abyssi) [Search protein sequence]
MNAVEIISRDIYKAIDIQTKILDYMTKFFTDRGFKWLLPIMLSPITDPLW
PDPIRPAEVDVYGVRMRLTHSMILHKQLAIAMGLEKIFVLSPNIRLESRR
KDDGRHSYEFTQLDFEIEGAKMKDVMRLIEELIYGLFRKAEEWTGREFPR
ARHFKVYDYKDILEEFGSDEKASMEMEEPFWIVNIPREFYDREENGVWKN
YDLILPYGYGEVSSGGEREWEYEKIVAKIRAAGLKEDSFRPYLEIARAGK
LKPSAGAGIGVERLVRFIVGAKHIAEVQPFPRVPGIPAVI
3D structure
PDB3rex Crystal Structure of the Archaeal Asparagine Synthetase: Interrelation with Aspartyl-tRNA and Asparaginyl-tRNA Synthetases.
ChainB
Resolution1.8 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) R95 E97 R105 H106
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 B R99 H110 S111 F114 Q116 E215 V216 S217 G264 R267 R95 H106 S107 F110 Q112 E211 V212 S213 G260 R263
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:3rex, PDBe:3rex, PDBj:3rex
PDBsum3rex
PubMed21820443
UniProtQ9V228

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