Structure of PDB 2d74 Chain A

Receptor sequence
>2d74A (length=403) Species: 186497 (Pyrococcus furiosus DSM 3638) [Search protein sequence]
KTRQAEVNIGMVGHVDHGKTTLTKALTGVWTDTLRRGITIKIGFADAEIR
RCSNCGRYSTSPICPYCGHETEFIRRVSFIDSPGHEALMTTMLAGASLMD
GAILVIAANEPCPRPQTREHLMALQIIGQKNIIIAQNKIELVDKEKALEN
YRQIKEFIKGTVAENAPIIPISALHGANIDVLVKAIEEFIPTPKRDSNKP
PKMLVLRSFDVNKPGTPPEKLVGGVLDGSIVQGKLKVGDEIEIRPGVPYE
EHGRIKYEPITTEIVSLQAGGQFVEEAYPGGLVGIGTKLDPYLTKGDLMA
GNVVGKPGKLPPVWTDLRLEVHLLERVVGTEQELNVEPIKRKEVLLLNVG
TARTMGLVTALGKDEIELKLQIPVCAEPGERVAISRQIGSRWRLIGYGII
KEL
3D structure
PDB2d74 Structure of archaeal translational initiation factor 2 betagamma-GDP reveals significant conformational change of the beta-subunit and switch 1 region.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D21 K24 T25 T48 H94
Catalytic site (residue number reindexed from 1) D16 K19 T20 T39 H85
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 ZN A C61 C64 C73 C76 C52 C55 C64 C67
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
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:2d74, PDBe:2d74, PDBj:2d74
PDBsum2d74
PubMed16924118
UniProtQ8U082|IF2G_PYRFU Translation initiation factor 2 subunit gamma (Gene Name=eif2g)

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