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7PPZ

Crystal structure of the Burkholderia Lethal Factor 1 (BLF1) C94S inactive mutant in complex with human eIF4A - Crystal form A

Functional Information from GO Data
ChainGOidnamespacecontents
A0039606biological_processsymbiont-mediated suppression of host translation initiation
A0051097biological_processnegative regulation of helicase activity
B0000166molecular_functionnucleotide binding
B0000339molecular_functionRNA cap binding
B0002183biological_processcytoplasmic translational initiation
B0003676molecular_functionnucleic acid binding
B0003723molecular_functionRNA binding
B0003724molecular_functionRNA helicase activity
B0003725molecular_functiondouble-stranded RNA binding
B0003729molecular_functionmRNA binding
B0003743molecular_functiontranslation initiation factor activity
B0004386molecular_functionhelicase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006412biological_processtranslation
B0006413biological_processtranslational initiation
B0008135molecular_functiontranslation factor activity, RNA binding
B0010494cellular_componentcytoplasmic stress granule
B0016020cellular_componentmembrane
B0016281cellular_componenteukaryotic translation initiation factor 4F complex
B0016787molecular_functionhydrolase activity
B0016887molecular_functionATP hydrolysis activity
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0048471cellular_componentperinuclear region of cytoplasm
B0070062cellular_componentextracellular exosome
B0097165cellular_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
BVAL180-LEU188

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI2
Number of Residues28
DetailsMotif: {"description":"Q motif"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsMotif: {"description":"DEAD box"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P60843","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P60843","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues6
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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