Structure of PDB 5h7l Chain A

Receptor sequence
>5h7lA (length=694) Species: 70601 (Pyrococcus horikoshii OT3) [Search protein sequence]
AKIKELMLQPERIRNIGIAAHIDHGKTTLSDNLLAGAGMNAANVSMVHNY
EGKDYLINLIDTPGHVDFGGDVTRAMRAIDGVIIVVDAVEGVMPQTETVV
RQALREYVKPVLFINKVDRLIRELKLTPQQMMERFSKIIMDVNRLIQRYA
PEEYKKKWMVKVEDGSVAFGSAYYNWALSVPFMKRTGVKFNEIIDLTLKG
DNRTLRQKAPLHVVVLDMVVRHLPSPIEAQKYRIPHLWEGDISSDIGQAM
LNCDPKGKMVMVVTKIIGEVATGRVWSGTVKSGQEVYLINTKRKARIQQV
GIYMGPERINMEAVPAGNIVAVTGLRDAMAGETVAEEQIEPFEALHYVSE
PVVTVAIEAKNVKDLPRLIEALRQLAKEDPTLHVKIDEETGQHLLSGMGE
LHLEVKLYKLKKDWGIDIEVSEPIVVYRESITKSSPMVEGKSPNRHNRFY
IVVEPMPDEIYNAIKEGIIPEGRVKNPKEVAKKLAELGMDYEIARGIVDI
YNGNMFIDNTKGVQYLNEVMDLLIDGFHQAMDEGPLAREPVMKVIVRLLD
AQVHEDNVHRGPAQIYPAIRTAIHCAMMKSNPVLYEPYQKVIINIPYEYM
GAVSREITQRRGQLVDMKQEGEVMTIIAEAPVAEMFGFAGSIRSATSGRA
LWSTEHAGFKRVPNELAQQIIRQIRQRKGLDPNPPTEKDVCPLF
3D structure
PDB5h7l The C-terminal helix of ribosomal P stalk recognizes a hydrophobic groove of elongation factor 2 in a novel fashion
ChainA
Resolution3.1 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 ?
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 peptide A P164 M168 V198 E199 F205 M219 K225 F226 P128 M132 V162 E163 F169 M183 K189 F190
Gene Ontology
Molecular Function
GO:0003746 translation elongation factor activity
GO:0003924 GTPase activity
GO:0005525 GTP binding
Biological Process
GO:0006412 translation
GO:0006414 translational elongation
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:5h7l, PDBe:5h7l, PDBj:5h7l
PDBsum5h7l
PubMed29471537
UniProtO59521|EF2_PYRHO Elongation factor 2 (Gene Name=fusA)

[Back to BioLiP]