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4CXH

Regulation of the mammalian elongation cycle by 40S subunit rolling: a eukaryotic-specific ribosome rearrangement

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003746molecular_functiontranslation elongation factor activity
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0006412biological_processtranslation
A0006414biological_processtranslational elongation
A0006790biological_processsulfur compound metabolic process
X0002181biological_processcytoplasmic translation
X0003723molecular_functionRNA binding
X0003735molecular_functionstructural constituent of ribosome
X0005515molecular_functionprotein binding
X0005634cellular_componentnucleus
X0005654cellular_componentnucleoplasm
X0005730cellular_componentnucleolus
X0005737cellular_componentcytoplasm
X0005783cellular_componentendoplasmic reticulum
X0005791cellular_componentrough endoplasmic reticulum
X0005829cellular_componentcytosol
X0005840cellular_componentribosome
X0006412biological_processtranslation
X0015935cellular_componentsmall ribosomal subunit
X0016020cellular_componentmembrane
X0022626cellular_componentcytosolic ribosome
X0022627cellular_componentcytosolic small ribosomal subunit
X0032040cellular_componentsmall-subunit processome
X0034063biological_processstress granule assembly
X0042274biological_processribosomal small subunit biogenesis
X0045202cellular_componentsynapse
X1990145biological_processmaintenance of translational fidelity
X1990904cellular_componentribonucleoprotein complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PHE Y 77
ChainResidue
ATYR241
AVAL251
AGLY296
YA76

Functional Information from PROSITE/UniProt
site_idPS00301
Number of Residues16
DetailsG_TR_1 Translational (tr)-type guanine nucleotide-binding (G) domain signature. DKmkeEReRGITIdlT
ChainResidueDetails
AASP60-THR75

site_idPS00055
Number of Residues8
DetailsRIBOSOMAL_S12 Ribosomal protein S12 signature. KqPNSAiR
ChainResidueDetails
XLYS60-ARG67

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P62267
ChainResidueDetails
XLYS54
AASP90
AASN152

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: 3-hydroxyproline => ECO:0000269|PubMed:24550447, ECO:0000269|PubMed:24550462, ECO:0000269|PubMed:28257692
ChainResidueDetails
XPRO62

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
XLYS135

site_idSWS_FT_FI4
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
XLYS37

218853

PDB entries from 2024-04-24

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