Structure of PDB 2efg Chain A

Receptor sequence
>2efgA (length=582) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
YDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIAAVTTCFWKDHRINIID
TPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSETVWRQAEKYKVPRI
AFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDVLRM
KAYTYGNDLGTDIREIPIPEEYLDNAREYHEKLVEVAADFDENIMLKYLE
GEEPTEEELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSP
LDIPPIKGTTPEGEVVEIHPDPNGPLAALAFKIMADPYVGRLTFIRVYSG
TLTSGSYVYNTTKGRKERVARLLRMHANHREEVEELKAGDLGAVVGLKET
ITGDTLVGEDAPRVILESVGKPQVAYRETITKPVDVEGKFIRQTGGRGQY
GHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIPAVQKGIEEAMQSGPLIG
FPVVDIKVTLYDGSYHEVDSSEMAFKIAGSMAIKEAVQKGDPVILEPIMR
VEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYAT
DLRSKTQGRGSFVMFFDHYQEVPKQVQEKLIK
3D structure
PDB2efg The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution.
ChainA
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) D22
Catalytic site (residue number reindexed from 1) D16
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 GDP A D22 G24 K25 T26 T27 N137 K138 D140 S262 L264 D16 G18 K19 T20 T21 N104 K105 D107 S229 L231
Gene Ontology
Molecular Function
GO:0003746 translation elongation factor activity
GO:0003924 GTPase activity
GO:0005525 GTP binding
Biological Process
GO:0006412 translation
GO:0006414 translational elongation
GO:0032790 ribosome disassembly
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2efg, PDBe:2efg, PDBj:2efg
PDBsum2efg
PubMed8070396
UniProtQ5SHN5|EFG_THET8 Elongation factor G (Gene Name=fusA)

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