Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3EIQ

Crystal structure of Pdcd4-eIF4A

Functional Information from GO Data
ChainGOidnamespacecontents
A0000339molecular_functionRNA cap binding
A0002183biological_processcytoplasmic translational initiation
A0003676molecular_functionnucleic acid binding
A0003723molecular_functionRNA binding
A0003724molecular_functionRNA helicase activity
A0003725molecular_functiondouble-stranded RNA binding
A0003729molecular_functionmRNA binding
A0003743molecular_functiontranslation initiation factor activity
A0004386molecular_functionhelicase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006412biological_processtranslation
A0006413biological_processtranslational initiation
A0008135molecular_functiontranslation factor activity, RNA binding
A0016020cellular_componentmembrane
A0016281cellular_componenteukaryotic translation initiation factor 4F complex
A0016787molecular_functionhydrolase activity
A0016887molecular_functionATP hydrolysis activity
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0048471cellular_componentperinuclear region of cytoplasm
A0070062cellular_componentextracellular exosome
A0097165cellular_componentnuclear stress granule
C0045892biological_processnegative regulation of DNA-templated transcription
D0000339molecular_functionRNA cap binding
D0002183biological_processcytoplasmic translational initiation
D0003676molecular_functionnucleic acid binding
D0003723molecular_functionRNA binding
D0003724molecular_functionRNA helicase activity
D0003725molecular_functiondouble-stranded RNA binding
D0003729molecular_functionmRNA binding
D0003743molecular_functiontranslation initiation factor activity
D0004386molecular_functionhelicase activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0006412biological_processtranslation
D0006413biological_processtranslational initiation
D0008135molecular_functiontranslation factor activity, RNA binding
D0016020cellular_componentmembrane
D0016281cellular_componenteukaryotic translation initiation factor 4F complex
D0016787molecular_functionhydrolase activity
D0016887molecular_functionATP hydrolysis activity
D0045944biological_processpositive regulation of transcription by RNA polymerase II
D0048471cellular_componentperinuclear region of cytoplasm
D0070062cellular_componentextracellular exosome
D0097165cellular_componentnuclear stress granule
Functional Information from PROSITE/UniProt
site_idPS00039
Number of Residues9
DetailsDEAD_ATP_HELICASE DEAD-box subfamily ATP-dependent helicases signature. VLDEADEmL
ChainResidueDetails
AVAL180-LEU188

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q53EL6
ChainResidueDetails
CTYR152
DALA76

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079
ChainResidueDetails
CSER313
DSER2

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q53EL6
ChainResidueDetails
CSER317
DSER4

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKB => ECO:0000250|UniProtKB:Q53EL6
ChainResidueDetails
CSER457
ALYS174
DLYS118
DLYS174

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR158
DTHR158

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P60843
ChainResidueDetails
ALYS193
DLYS193

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P60843
ChainResidueDetails
ALYS238
DLYS238

site_idSWS_FT_FI8
Number of Residues12
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS146
DLYS309
DLYS369
DLYS381
ALYS225
ALYS309
ALYS369
ALYS381
DLYS146
DLYS225

site_idSWS_FT_FI9
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS238
DLYS238

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon