Home Research COVID-19 Services Publications People Teaching Job Opening News Forum Lab Only
Online Services

I-TASSER I-TASSER-MTD C-I-TASSER CR-I-TASSER QUARK C-QUARK LOMETS MUSTER CEthreader SEGMER DeepFold DeepFoldRNA FoldDesign COFACTOR COACH MetaGO TripletGO IonCom FG-MD ModRefiner REMO DEMO DEMO-EM SPRING COTH Threpp PEPPI BSpred ANGLOR EDock BSP-SLIM SAXSTER FUpred ThreaDom ThreaDomEx EvoDesign BindProf BindProfX SSIPe GPCR-I-TASSER MAGELLAN ResQ STRUM DAMpred

TM-score TM-align US-align MM-align RNA-align NW-align LS-align EDTSurf MVP MVP-Fit SPICKER HAAD PSSpred 3DRobot MR-REX I-TASSER-MR SVMSEQ NeBcon ResPRE TripletRes DeepPotential WDL-RF ATPbind DockRMSD DeepMSA FASPR EM-Refiner GPU-I-TASSER

BioLiP E. coli GLASS GPCR-HGmod GPCR-RD GPCR-EXP Tara-3D TM-fold DECOYS POTENTIAL RW/RWplus EvoEF HPSF THE-DB ADDRESS Alpaca-Antibody CASP7 CASP8 CASP9 CASP10 CASP11 CASP12 CASP13 CASP14

BioLiP

Structure of PDB 2p8z Chain T

Receptor sequence
>2p8zT (length=814) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
AFTVDQMRSLMDKVTNVRNMSVIAHVDHGKSTLTDSLVQRAGIISAGITI
KSTAISLYSEMSDEDVKEIKQKTDGNSFLINLIDSPGHVDFSSEVTAALR
VTDGALVVVDTIEGVCVQTETVLRQALGERIKPVVVINKVDRALLELQVS
KEDLYQTFARTVESVNVIVSTYADEVLGDVQVYPARGTVAFGSGLHGWAF
TIRQFATRYAKKFGVDKAKMMDRLWGDSFFNPKTKKWTNKDTDAEGKPLE
RAFNMFILDPIFRLFTAIMNFKKDEIPVLLEKLEIVLKGDEKDLEGKALL
KVVMRKFLPAADALLEMIVLHLPSPVTAQAYRAEQLYEGPADDANCIAIK
NCDPKADLMLYVSKMVPTSDKGRFYAFGRVFAGTVKSGQKVRIQGPNYVP
GKKDDLFIKAIQRVVLMMGRFVEPIDDCPAGNIIGLVGIDQFLLKTGTLT
TSETAHNMKVMKFSVSPVVQVAVEVKNANDLPKLVEGLKRLSKSDPCVLT
YMSESGEHIVAGTGELHLEICLQDLEHDHAGVPLKISPPVVAYRETVESE
SSQTALSKSPNKHNRIYLKAEPIDEEVSLAIENGIINPRDDFKARARIMA
DDYGWDVTDARKIWCFGPDGNGPNLVIDQTKAVQYLHEIKDSVVAAFQWA
TKEGPIFGEEMRSVRVNILDVTLHADAIHRGGGQIIPTMRRATYAGFLLA
DPKILVEIQCPEQAVGGIYSVLNKKRGQVVSEEQTPLFTVKAYLPVNESF
GFTGELRQATGGQAFPQMVFDHWSTLGSDPLDPTSKAGEIVLAARKRHGM
KEEVPGWQEYYDKL
3D structure
PDB2p8z Structures of modified eEF2.80S ribosome complexes reveal the role of GTP hydrolysis in translocation.
ChainT
Resolution8.9 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 3.6.5.-
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 APR T H694 D696 I698 X699 H674 D676 I678 X679
BS02 SO1 T P559 V561 F798 P539 V541 F770
BS03 GNP T H27 V28 D29 H30 G31 K32 T34 K159 D161 S213 G214 L215 H216 H25 V26 D27 H28 G29 K30 T32 K139 D141 S193 G194 L195 H196
Gene Ontology
Molecular Function
GO:0003746 translation elongation factor activity
GO:0003924 GTPase activity
GO:0005515 protein binding
GO:0005525 GTP binding
GO:0016787 hydrolase activity
GO:0019843 rRNA binding
GO:0042802 identical protein binding
GO:0043022 ribosome binding
GO:0051087 protein-folding chaperone binding
Biological Process
GO:0006412 translation
GO:0006414 translational elongation
GO:0045901 positive regulation of translational elongation
GO:1990145 maintenance of translational fidelity
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:1990904 ribonucleoprotein complex

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:2p8z, PDBe:2p8z, PDBj:2p8z
PDBsum2p8z
PubMed17446867
UniProtP32324|EF2_YEAST Elongation factor 2 (Gene Name=EFT1)

[Back to BioLiP]

zhanglabzhanggroup.org | +65-6601-1241 | Computing 1, 13 Computing Drive, Singapore 117417