Structure of PDB 2iwh Chain B

Receptor sequence
>2iwhB (length=980) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
HHHHSDSQQSIKVLEELFQKLSVATADNRHEIASEVASFLNGNIIEHDVP
EHFFGELAKGIKDKKTAANAMQAVAHIANQSNLSPSVEPYIVQLVPAICT
NAGNKDKEIQSVASETLISIVNAVNPVAIKALLPHLTNAIVETNKWQEKI
AILAAFSAMVDAAKDQVALRMPELIPVLSETMWDTKKEVKAAATAAMTKA
TETVDNKDIERFIPSLIQCIADPTEVPETVHLLGATTFVAEVTPATLSIM
VPLLSRGLNERETGIKRKSAVIIDNMCKLVEDPQVIAPFLGKLLPGLKSN
FATIADPEAREVTLRALKTLRRVGNVGEDDAIPELSHAGDVSTTLQVVNE
LLKDETVAPRFKIVVEYIAAIGADLIDERIIDQQAWFTHITPYMTIFLHE
KKAKDILDEFRKRAVDNIPVGPNFDDEEDEGEDLCNCEFSLAYGAKILLN
KTQLRLKRARRYGICGPNGCGKSTLMRAIANGQVDGFPTQEECRTVYVEH
DIDGTHSDTSVLDFVFESGVGTKEAIKDKLIEFGFTDEMIAMPISALSGG
WKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYLNTCGITSITIS
HDSVFLDNVCEYIINYEGLKLRKYKGNFTEFVKKCPAAKAYEELSNTDLE
FKFPEPGYLEGVKTKQKAIVKVTNMEFQYPGTSKPQITDINFQCSLSSRI
AVIGPNGAGKSTLINVLTGELLPTSGEVYTHENCRIAYIKQHAFAHIESH
LDKTPSEYIQWRFQTGEDRETMDRANRQINENDAEAMNKIFKIEGTPRRI
AGIHSRRKFKNTYEYECSFLLGENIGMKSERWVPMMSVDNAWIPRGELVE
SHSKMVAEVDMKEALASGQFRPLTRKEIEEHCSMLGLDPEIVSHSRIRGL
SGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEFEGGVI
IITHSAEFTKNLTEEVWAVKDGRMTPSGHN
3D structure
PDB2iwh Structure of Eef3 and the Mechanism of Transfer RNA Release from the E-Site.
ChainB
Resolution3.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.6.4.-
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 ANP B I41 H43 D44 S82 T391 I392 H395 E396 N702 E921 N924 H950 I45 H47 D48 S86 T395 I396 H399 E400 N706 E925 N928 H954
Gene Ontology
Molecular Function
GO:0003746 translation elongation factor activity
GO:0005524 ATP binding
GO:0016787 hydrolase activity
GO:0016887 ATP hydrolysis activity
GO:0019843 rRNA binding
GO:0043022 ribosome binding
Biological Process
GO:0001933 negative regulation of protein phosphorylation
GO:0006412 translation
GO:0006414 translational elongation
GO:0006415 translational termination
GO:0006469 negative regulation of protein kinase activity
Cellular Component
GO:0005737 cytoplasm
GO:0005840 ribosome
GO:0010494 cytoplasmic stress granule
GO:0022626 cytosolic ribosome

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:2iwh, PDBe:2iwh, PDBj:2iwh
PDBsum2iwh
PubMed16929303
UniProtP16521|EF3A_YEAST Elongation factor 3A (Gene Name=YEF3)

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