Structure of PDB 2p8y Chain T Binding Site BS01
Receptor Information
>2p8y 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
APR
InChI
InChI=1S/C15H23N5O14P2/c16-12-7-13(18-3-17-12)20(4-19-7)14-10(23)8(21)5(32-14)1-30-35(26,27)34-36(28,29)31-2-6-9(22)11(24)15(25)33-6/h3-6,8-11,14-15,21-25H,1-2H2,(H,26,27)(H,28,29)(H2,16,17,18)/t5-,6-,8-,9-,10-,11-,14-,15-/m1/s1
InChIKey
SRNWOUGRCWSEMX-KEOHHSTQSA-N
SMILES
Software
SMILES
ACDLabs 10.04
O=P(O)(OCC3OC(n1c2ncnc(N)c2nc1)C(O)C3O)OP(=O)(O)OCC4OC(O)C(O)C4O
OpenEye OEToolkits 1.5.0
c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)O[P@](=O)(O)OC[C@@H]4[C@H]([C@H]([C@@H](O4)O)O)O)O)O)N
OpenEye OEToolkits 1.5.0
c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OCC4C(C(C(O4)O)O)O)O)O)N
CACTVS 3.341
Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)OC[CH]4O[CH](O)[CH](O)[CH]4O)[CH](O)[CH]3O
CACTVS 3.341
Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P@@](O)(=O)OC[C@H]4O[C@@H](O)[C@H](O)[C@@H]4O)[C@@H](O)[C@H]3O
Formula
C15 H23 N5 O14 P2
Name
ADENOSINE-5-DIPHOSPHORIBOSE
ChEMBL
CHEMBL1231026
DrugBank
ZINC
ZINC000017654550
PDB chain
2p8y Chain T Residue 1699 [
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Receptor-Ligand Complex Structure
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PDB
2p8y
Structures of modified eEF2.80S ribosome complexes reveal the role of GTP hydrolysis in translocation.
Resolution
11.7 Å
Binding residue
(original residue number in PDB)
H694 D696 I698 X699
Binding residue
(residue number reindexed from 1)
H674 D676 I678 X679
Annotation score
2
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:2p8y
,
PDBe:2p8y
,
PDBj:2p8y
PDBsum
2p8y
PubMed
17446867
UniProt
P32324
|EF2_YEAST Elongation factor 2 (Gene Name=EFT1)
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