Structure of PDB 3cw2 Chain B

Receptor sequence
>3cw2B (length=400) Species: 2287 (Saccharolobus solfataricus) [Search protein sequence]
AWPKVQPEVNIGVVGHVDHGKTTLVQAITGIWTSTIKLGYAETNIGVCES
CKKPEAYVTEPSCKSCGSDDEPKFLRRISFIDAPGHEVLMATMLSGAALM
DGAILVVAANEPFPQPQTREHFVALGIIGVKNLIIVQNKVDVVSKEEALS
QYRQIKQFTKGTWAENVPIIPVSALHKINIDSLIEGIEEYIKTPYRDLSQ
KPVMLVIRSFDVNKPGTQFNELKGGVIGGSIIQGLFKVDQEIKVLPGLRV
EKQGKVSYEPIFTKISSIRFGDEEFKEAKPGGLVAIGTYLDPSLTKADNL
LGSIITLADAEVPVLWNIRIKYNLLGAKEMLKVDPIRAKETLMLSVGSST
TLGIVTSVKKDEIEVELRRPVAVWSNNIRTVISRQIAGRWRMIGWGLVEI
3D structure
PDB3cw2 Crystal structure of the intact archaeal translation initiation factor 2 demonstrates very high conformational flexibility in the alpha- and beta-subunits.
ChainB
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) D19 K22 T23 T46 H97
Catalytic site (residue number reindexed from 1) D18 K21 T22 T35 H86
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 peptide B E66 V151 Y163 K167 P182 V183 I189 N190 D192 E55 V140 Y152 K156 P171 V172 I178 N179 D181
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:3cw2, PDBe:3cw2, PDBj:3cw2
PDBsum3cw2
PubMed18675278
UniProtQ980A5|IF2G_SACS2 Translation initiation factor 2 subunit gamma (Gene Name=eif2g)

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