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5ZC9

Crystal structure of the human eIF4A1-ATP analog-RocA-polypurine RNA complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
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
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
A0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues30
Detailsbinding site for residue ANP A 500
ChainResidue
APHE52
AGLU183
AGLY335
AASP337
AGLN339
AARG362
AARG365
APHE366
AMG501
AHOH606
AHOH613
ALYS54
AHOH618
AHOH621
AHOH626
AHOH627
AHOH629
AHOH673
AHOH702
AHOH713
AHOH726
AHOH732
AGLN59
AHOH746
ASER78
AGLY79
ATHR80
AGLY81
ALYS82
ATHR83

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 501
ChainResidue
AANP500
AHOH613
AHOH618
AHOH629
AHOH673

site_idAC3
Number of Residues10
Detailsbinding site for residue RCG B 600
ChainResidue
APRO159
APHE163
AGLN195
AASP198
BA7
BG8
BHOH701
BHOH702
BHOH708
BHOH724

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
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00541
ChainResidueDetails
AALA76

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS118
ALYS174

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR158

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P60843
ChainResidueDetails
ALYS193

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P60843
ChainResidueDetails
ALYS238

site_idSWS_FT_FI6
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS146
ALYS225
ALYS309
ALYS369
ALYS381

site_idSWS_FT_FI7
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS238

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PDB entries from 2024-04-24

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