3EIQ
Crystal structure of Pdcd4-eIF4A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000339 | molecular_function | RNA cap binding |
| A | 0002183 | biological_process | cytoplasmic translational initiation |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0003723 | molecular_function | RNA binding |
| A | 0003724 | molecular_function | RNA helicase activity |
| A | 0003725 | molecular_function | double-stranded RNA binding |
| A | 0003729 | molecular_function | mRNA binding |
| A | 0003743 | molecular_function | translation initiation factor activity |
| A | 0004386 | molecular_function | helicase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006412 | biological_process | translation |
| A | 0006413 | biological_process | translational initiation |
| A | 0008135 | molecular_function | translation factor activity, RNA binding |
| A | 0010494 | cellular_component | cytoplasmic stress granule |
| A | 0016020 | cellular_component | membrane |
| A | 0016281 | cellular_component | eukaryotic translation initiation factor 4F complex |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
| A | 0048471 | cellular_component | perinuclear region of cytoplasm |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0097165 | cellular_component | nuclear stress granule |
| C | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0000339 | molecular_function | RNA cap binding |
| D | 0002183 | biological_process | cytoplasmic translational initiation |
| D | 0003676 | molecular_function | nucleic acid binding |
| D | 0003723 | molecular_function | RNA binding |
| D | 0003724 | molecular_function | RNA helicase activity |
| D | 0003725 | molecular_function | double-stranded RNA binding |
| D | 0003729 | molecular_function | mRNA binding |
| D | 0003743 | molecular_function | translation initiation factor activity |
| D | 0004386 | molecular_function | helicase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005634 | cellular_component | nucleus |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0006412 | biological_process | translation |
| D | 0006413 | biological_process | translational initiation |
| D | 0008135 | molecular_function | translation factor activity, RNA binding |
| D | 0010494 | cellular_component | cytoplasmic stress granule |
| D | 0016020 | cellular_component | membrane |
| D | 0016281 | cellular_component | eukaryotic translation initiation factor 4F complex |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
| D | 0048471 | cellular_component | perinuclear region of cytoplasm |
| D | 0070062 | cellular_component | extracellular exosome |
| D | 0097165 | cellular_component | nuclear stress granule |
Functional Information from PROSITE/UniProt
| site_id | PS00039 |
| Number of Residues | 9 |
| Details | DEAD_ATP_HELICASE DEAD-box subfamily ATP-dependent helicases signature. VLDEADEmL |
| Chain | Residue | Details |
| A | VAL180-LEU188 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 342 |
| Details | Domain: {"description":"Helicase ATP-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 56 |
| Details | Motif: {"description":"Q motif"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Motif: {"description":"DEAD box"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P60843","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P60843","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 11 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 123 |
| Details | Domain: {"description":"MI 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00698","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q53EL6","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
