Structure of PDB 2ywf Chain A

Receptor sequence
>2ywfA (length=532) Species: 224324 (Aquifex aeolicus VF5) [Search protein sequence]
MEQKNVRNFCIIAHVDHGKSTLADRLLEYTGAIGITVKMQAVRMFYKAKD
GNTYKLHLIDTPGHVDFSYEVSRALAACEGALLLIDASQGIEAQTVANFW
KAVEQDLVIIPVINKIDLPSADVDRVKKQIEEVLGLDPEEAILASAKEGI
GIEEILEAIVNRIPPPKGDPQKPLKALIFDSYYDPYRGAVAFVRIFDGEV
KPGDKIMLMSTGKEYEVTEVGAQTPKMTKFDKLSAGDVGYIAASIKDVRD
IRIGDTITHAKNPTKEPVPGFQPAKPMVYAGIYPAEDTTYEELRDALEKY
AINDAAIVYEPESSPALGMGFRVGFLGLLHMEIVQERLEREYGVKIITTA
PNVIYRVKKKFTDEVIEVRNPMDFPDNAGLIEYVEEPFVLVTIITPKEYV
GPIIQLCQEKRGIQKNMTYLDPNTVYLEYEMPLSEIIVDFHDKIKSISRG
FASYDYEFIGYRPSDLIKLTVLINKKPVDALSFIVHADRAQKFARRVAEK
LRETIPRQLFEVHIQVAKGGKVIASERIKPLR
3D structure
PDB2ywf Crystal structures of GTP-binding protein LepA from Aquifex aeolicus
ChainA
Resolution2.24 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D16
Catalytic site (residue number reindexed from 1) D16
Enzyme Commision number 3.6.5.n1: elongation factor 4.
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 GNP A V15 D16 G18 K19 S20 T21 N133 K134 D136 L137 S164 K166 V15 D16 G18 K19 S20 T21 N114 K115 D117 L118 S145 K147
Gene Ontology
Molecular Function
GO:0003746 translation elongation factor activity
GO:0003924 GTPase activity
GO:0005525 GTP binding
GO:0016787 hydrolase activity
GO:0043022 ribosome binding
Biological Process
GO:0006412 translation
GO:0006414 translational elongation
GO:0045727 positive regulation of translation
Cellular Component
GO:0005886 plasma membrane

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Cellular Component
External links
PDB RCSB:2ywf, PDBe:2ywf, PDBj:2ywf
PDBsum2ywf
PubMed
UniProtO67618|LEPA_AQUAE Elongation factor 4 (Gene Name=lepA)

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