Structure of PDB 5jup Chain DC Binding Site BS04
Receptor Information
>5jup Chain DC (length=824) Species:
4932
(Saccharomyces cerevisiae) [
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VAFTVDQMRSLMDKVTNVRNMSVIAHVDHGKSTLTDSLVQRAGIISAAGI
TIKSTAISLYSEMSDEDVKEIKQKTDGNSFLINLIDSPGHVDFSSEVTAA
LRVTDGALVVVDTIEGVCVQTETVLRQALGERIKPVVVINKVDRALLELQ
VSKEDLYQTFARTVESVNVIVSTYADEVLGDVQVYPARGTVAFGSGLHGW
AFTIRQFATRYAKKFGVDKAKMMDRLWGDSFFNPKTKKWTNKDTDAEGKP
LERAFNMFILDPIFRLFTAIMNFKKDEIPVLLEKLEIVLKGDEKDLEGKA
LLKVVMRKFLPAADALLEMIVLHLPSPVTAQAYRAEQLYEGPADDANCIA
IKNCDPKADLMLYVSKMVPTSDKGRFYAFGRVFAGTVKSGQKVRIQGPNY
VPGKKDDLFIKAIQRVVLMMGRFVEPIDDCPAGNIIGLVGIDQFLLKTGT
LTTSETAHNMKVMKFSVSPVVQVAVEVKNANDLPKLVEGLKRLSKSDPCV
LTYMSESGEHIVAGTGELHLEICLQDLEHDHAGVPLKISPPVVAYRETVE
SESSQTALSKSPNKHNRIYLKAEPIDEEVSLAIENGIINPRDDFKARARI
MADDYGWDVTDARKIWCFGPDGNGPNLVIDQTKAVQYLHEIKDSVVAAFQ
WATKEGPIFGEEMRSVRVNILDVTLHADAIHRGGGQIIPTMRRATYAGFL
LADPKIQEPVFLVEIQCPEQAVGGIYSVLNKKRGQVVSEEQRPGTPLFTV
KAYLPVNESFGFTGELRQATGGQAFPQMVFDHWSTLGSDPLDPTSKAGEI
VLAARKRHGMKEEVPGWQEYYDKL
Ligand information
Ligand ID
GDP
InChI
InChI=1S/C10H15N5O11P2/c11-10-13-7-4(8(18)14-10)12-2-15(7)9-6(17)5(16)3(25-9)1-24-28(22,23)26-27(19,20)21/h2-3,5-6,9,16-17H,1H2,(H,22,23)(H2,19,20,21)(H3,11,13,14,18)/t3-,5-,6-,9-/m1/s1
InChIKey
QGWNDRXFNXRZMB-UUOKFMHZSA-N
SMILES
Software
SMILES
OpenEye OEToolkits 1.7.6
c1nc2c(n1C3C(C(C(O3)COP(=O)(O)OP(=O)(O)O)O)O)N=C(NC2=O)N
CACTVS 3.385
NC1=Nc2n(cnc2C(=O)N1)[C@@H]3O[C@H](CO[P](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
CACTVS 3.385
NC1=Nc2n(cnc2C(=O)N1)[CH]3O[CH](CO[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 12.01
O=P(O)(O)OP(=O)(O)OCC3OC(n2cnc1c2N=C(N)NC1=O)C(O)C3O
OpenEye OEToolkits 1.7.6
c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)OP(=O)(O)O)O)O)N=C(NC2=O)N
Formula
C10 H15 N5 O11 P2
Name
GUANOSINE-5'-DIPHOSPHATE
ChEMBL
CHEMBL384759
DrugBank
DB04315
ZINC
ZINC000008215481
PDB chain
5jup Chain DC Residue 901 [
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Receptor-Ligand Complex Structure
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PDB
5jup
Ensemble cryo-EM uncovers inchworm-like translocation of a viral IRES through the ribosome.
Resolution
3.5 Å
Binding residue
(original residue number in PDB)
V28 D29 G31 K32 S33 T34 N158 K159 D161 S213 L215
Binding residue
(residue number reindexed from 1)
V27 D28 G30 K31 S32 T33 N140 K141 D143 S195 L197
Annotation score
4
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
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Cellular Component
External links
PDB
RCSB:5jup
,
PDBe:5jup
,
PDBj:5jup
PDBsum
5jup
PubMed
27159452
UniProt
P32324
|EF2_YEAST Elongation factor 2 (Gene Name=EFT1)
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