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8QZZ

Crystal structure of human eIF2 alpha-gamma complexed with PPP1R15A_420-452

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0000166molecular_functionnucleotide binding
A0001731biological_processformation of translation preinitiation complex
A0002183biological_processcytoplasmic translational initiation
A0003743molecular_functiontranslation initiation factor activity
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005850cellular_componenteukaryotic translation initiation factor 2 complex
A0006412biological_processtranslation
A0006413biological_processtranslational initiation
A0006446biological_processregulation of translational initiation
A0008135molecular_functiontranslation factor activity, RNA binding
A0016787molecular_functionhydrolase activity
A0045296molecular_functioncadherin binding
A0070062cellular_componentextracellular exosome
A1990856molecular_functionmethionyl-initiator methionine tRNA binding
B0000423biological_processmitophagy
B0003676molecular_functionnucleic acid binding
B0003723molecular_functionRNA binding
B0003743molecular_functiontranslation initiation factor activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0005850cellular_componenteukaryotic translation initiation factor 2 complex
B0006412biological_processtranslation
B0006413biological_processtranslational initiation
B0006417biological_processregulation of translation
B0006446biological_processregulation of translational initiation
B0010494cellular_componentcytoplasmic stress granule
B0016020cellular_componentmembrane
B0032057biological_processnegative regulation of translational initiation in response to stress
B0033290cellular_componenteukaryotic 48S preinitiation complex
B0034063biological_processstress granule assembly
B0034198biological_processcellular response to amino acid starvation
B0034599biological_processcellular response to oxidative stress
B0034605biological_processcellular response to heat
B0034644biological_processcellular response to UV
B0034976biological_processresponse to endoplasmic reticulum stress
B0036490biological_processregulation of translation in response to endoplasmic reticulum stress
B0036499biological_processPERK-mediated unfolded protein response
B0043022molecular_functionribosome binding
B0044207cellular_componenttranslation initiation ternary complex
B0045202cellular_componentsynapse
B0070062cellular_componentextracellular exosome
B0097451cellular_componentglial limiting end-foot
B0140468biological_processHRI-mediated signaling
B0160296molecular_functioncap-dependent translation initiation factor activity
B0160297molecular_functionIRES-mediated translation initiation factor activity
B1904373biological_processresponse to kainic acid
B1990737biological_processresponse to manganese-induced endoplasmic reticulum stress
B2000676biological_processpositive regulation of type B pancreatic cell apoptotic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsRegion: {"description":"G1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01059","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsRegion: {"description":"G4","evidences":[{"source":"PROSITE-ProRule","id":"PRU01059","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsRegion: {"description":"G5","evidences":[{"source":"PROSITE-ProRule","id":"PRU01059","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsRegion: {"description":"Interacts with CDC123","evidences":[{"source":"PubMed","id":"35031321","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P32481","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9Z0N1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"24092754","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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