Structure of PDB 4rjl Chain A

Receptor sequence
>4rjlA (length=414) Species: 273057 (Saccharolobus solfataricus P2) [Search protein sequence]
AWPKVQPEVNIGVVGHVDHGKTTLVQAITGIWTSKHSEELKRGMTIKLGY
AETNIGVCESCKKPEAYVTEPSCKSCGSDDEPKFLRRISFIDAPGHEVLM
ATMLSGAALMDGAILVVAANEPFPQPQTREHFVALGIIGVKNLIIVQNKV
DVVSKEEALSQYRQIKQFTKGTWAENVPIIPVSALHKINIDSLIEGIEEY
IKTPYRDLSQKPVMLVIRSFDVNKPGTQFNELKGGVIGGSIIQGLFKVDQ
EIKVLPGLRVEKQGKVSYEPIFTKISSIRFGDEEFKEAKPGGLVAIGTYL
DPSLTKADNLLGSIITLADAEVPVLWNIRIKYNLLERVVGAKEMLKVDPI
RAKETLMLSVGSSTTLGIVTSVKKDEIEVELRRPVAVWSNNIRTVISRQI
AGRWRMIGWGLVEI
3D structure
PDB4rjl Crystal structure of gamma subunit of the translation initiation factor 2 from Sulfolobus solfataricus in complex with GDPCP at 1.64A resolution
ChainA
Resolution1.6401 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D19 K22 T23 T46 H97
Catalytic site (residue number reindexed from 1) D18 K21 T22 T45 H96
Enzyme Commision number 3.6.5.3: protein-synthesizing GTPase.
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 MG A T23 T46 T22 T45
BS02 MG A V151 V154 V150 V153
Gene Ontology
Molecular Function
GO:0000049 tRNA binding
GO:0003743 translation initiation factor activity
GO:0003746 translation elongation factor activity
GO:0003924 GTPase activity
GO:0005515 protein binding
GO:0005525 GTP binding
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0001731 formation of translation preinitiation complex
GO:0006412 translation
GO:0006413 translational initiation
GO:0006414 translational elongation

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Molecular Function
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Biological Process
External links
PDB RCSB:4rjl, PDBe:4rjl, PDBj:4rjl
PDBsum4rjl
PubMed
UniProtQ980A5|IF2G_SACS2 Translation initiation factor 2 subunit gamma (Gene Name=eif2g)

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