Structure of PDB 2p8z Chain T Binding Site BS03
Receptor Information
>2p8z Chain T (length=814) Species:
4932
(Saccharomyces cerevisiae) [
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AFTVDQMRSLMDKVTNVRNMSVIAHVDHGKSTLTDSLVQRAGIISAGITI
KSTAISLYSEMSDEDVKEIKQKTDGNSFLINLIDSPGHVDFSSEVTAALR
VTDGALVVVDTIEGVCVQTETVLRQALGERIKPVVVINKVDRALLELQVS
KEDLYQTFARTVESVNVIVSTYADEVLGDVQVYPARGTVAFGSGLHGWAF
TIRQFATRYAKKFGVDKAKMMDRLWGDSFFNPKTKKWTNKDTDAEGKPLE
RAFNMFILDPIFRLFTAIMNFKKDEIPVLLEKLEIVLKGDEKDLEGKALL
KVVMRKFLPAADALLEMIVLHLPSPVTAQAYRAEQLYEGPADDANCIAIK
NCDPKADLMLYVSKMVPTSDKGRFYAFGRVFAGTVKSGQKVRIQGPNYVP
GKKDDLFIKAIQRVVLMMGRFVEPIDDCPAGNIIGLVGIDQFLLKTGTLT
TSETAHNMKVMKFSVSPVVQVAVEVKNANDLPKLVEGLKRLSKSDPCVLT
YMSESGEHIVAGTGELHLEICLQDLEHDHAGVPLKISPPVVAYRETVESE
SSQTALSKSPNKHNRIYLKAEPIDEEVSLAIENGIINPRDDFKARARIMA
DDYGWDVTDARKIWCFGPDGNGPNLVIDQTKAVQYLHEIKDSVVAAFQWA
TKEGPIFGEEMRSVRVNILDVTLHADAIHRGGGQIIPTMRRATYAGFLLA
DPKILVEIQCPEQAVGGIYSVLNKKRGQVVSEEQTPLFTVKAYLPVNESF
GFTGELRQATGGQAFPQMVFDHWSTLGSDPLDPTSKAGEIVLAARKRHGM
KEEVPGWQEYYDKL
Ligand information
Ligand ID
GNP
InChI
InChI=1S/C10H17N6O13P3/c11-10-13-7-4(8(19)14-10)12-2-16(7)9-6(18)5(17)3(28-9)1-27-32(25,26)29-31(23,24)15-30(20,21)22/h2-3,5-6,9,17-18H,1H2,(H,25,26)(H3,11,13,14,19)(H4,15,20,21,22,23,24)/t3-,5-,6-,9-/m1/s1
InChIKey
UQABYHGXWYXDTK-UUOKFMHZSA-N
SMILES
Software
SMILES
ACDLabs 10.04
O=P(O)(O)NP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c2N=C(N)NC1=O)C(O)C3O
OpenEye OEToolkits 1.5.0
c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)O[P@@](=O)(NP(=O)(O)O)O)O)O)N=C(NC2=O)N
OpenEye OEToolkits 1.5.0
c1nc2c(n1C3C(C(C(O3)COP(=O)(O)OP(=O)(NP(=O)(O)O)O)O)O)N=C(NC2=O)N
CACTVS 3.341
NC1=Nc2n(cnc2C(=O)N1)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P@@](O)(=O)N[P](O)(O)=O)[C@@H](O)[C@H]3O
CACTVS 3.341
NC1=Nc2n(cnc2C(=O)N1)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)N[P](O)(O)=O)[CH](O)[CH]3O
Formula
C10 H17 N6 O13 P3
Name
PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
ChEMBL
CHEMBL1233085
DrugBank
DB02082
ZINC
ZINC000037868676
PDB chain
2p8z Chain T Residue 843 [
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Receptor-Ligand Complex Structure
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PDB
2p8z
Structures of modified eEF2.80S ribosome complexes reveal the role of GTP hydrolysis in translocation.
Resolution
8.9 Å
Binding residue
(original residue number in PDB)
H27 V28 D29 H30 G31 K32 T34 K159 D161 S213 G214 L215 H216
Binding residue
(residue number reindexed from 1)
H25 V26 D27 H28 G29 K30 T32 K139 D141 S193 G194 L195 H196
Annotation score
3
Enzymatic activity
Enzyme Commision number
3.6.5.-
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
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Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:2p8z
,
PDBe:2p8z
,
PDBj:2p8z
PDBsum
2p8z
PubMed
17446867
UniProt
P32324
|EF2_YEAST Elongation factor 2 (Gene Name=EFT1)
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