Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6XKI

Crystal structure of eIF4A-I in complex with RNA bound to des-MePateA, a pateamine A analog

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0002183biological_processcytoplasmic translational initiation
A0003676molecular_functionnucleic acid binding
A0003723molecular_functionRNA binding
A0003724molecular_functionRNA helicase activity
A0003725molecular_functiondouble-stranded RNA binding
A0003743molecular_functiontranslation initiation factor activity
A0004386molecular_functionhelicase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006412biological_processtranslation
A0006413biological_processtranslational initiation
A0010494cellular_componentcytoplasmic stress granule
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
A0097165cellular_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 Residues171
DetailsDomain: {"description":"Helicase ATP-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues161
DetailsDomain: {"description":"Helicase C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00542","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues28
DetailsMotif: {"description":"Q motif"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsMotif: {"description":"DEAD box"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P60842","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P60842","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues6
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P60842","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P60842","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

PDB statisticsPDBj update infoContact PDBjnumon