Structure of PDB 4m0l Chain D

Receptor sequence
>4m0lD (length=405) Species: 273057 (Saccharolobus solfataricus P2) [Search protein sequence]
AWPKVQPEVNIGVVGHVDHGKTTLVQAITGIWTSKTIKLGYAETNIGVCE
SCKKPEAYVTEPSCKSCGSDDEPKFLRRISFIDAPGHEVLMATMLSGAAL
MDGAILVVAANEPFPQPQTREHFVALGIIGVKNLIIVQNKVDVVSKEEAL
SQYRQIKQFTKGTWAENVPIIPVSALHKINIDSLIEGIEEYIKTPYRDLS
QKPVMLVIRSFDVNKPGTQFNELKGGVIGGSIIQGLFKVDQEIKVLPGLR
VEKQGKVSYEPIFTKISSIRFGDEEFKEAKPGGLVAIGTYLDPSLTKADN
LLGSIITLADAEVPVLWNIRIKYNLLERVVGAKEMLKVDPIRAKETLMLS
VGSSTTLGIVTSVKKDEIEVELRRPVAVWSNNIRTVISRQIAGRWRMIGW
GLVEI
3D structure
PDB4m0l Conformational transitions in the gamma subunit of the archaeal translation initiation factor 2.
ChainD
Resolution2.6 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 T36 H87
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 GDP D D19 G21 K22 T23 T24 N149 K150 D152 S184 L186 D18 G20 K21 T22 T23 N139 K140 D142 S174 L176
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:4m0l, PDBe:4m0l, PDBj:4m0l
PDBsum4m0l
PubMed24598735
UniProtQ980A5|IF2G_SACS2 Translation initiation factor 2 subunit gamma (Gene Name=eif2g)

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