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8A0E

CryoEM structure of DHS-eIF5A1 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006412biological_processtranslation
A0008216biological_processspermidine metabolic process
A0008284biological_processpositive regulation of cell population proliferation
A0008612biological_processpeptidyl-lysine modification to peptidyl-hypusine
A0016740molecular_functiontransferase activity
A0034038molecular_functiondeoxyhypusine synthase activity
A0042102biological_processpositive regulation of T cell proliferation
A0042593biological_processglucose homeostasis
A0042802molecular_functionidentical protein binding
A0046203biological_processspermidine catabolic process
A0051604biological_processprotein maturation
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006412biological_processtranslation
B0008216biological_processspermidine metabolic process
B0008284biological_processpositive regulation of cell population proliferation
B0008612biological_processpeptidyl-lysine modification to peptidyl-hypusine
B0016740molecular_functiontransferase activity
B0034038molecular_functiondeoxyhypusine synthase activity
B0042102biological_processpositive regulation of T cell proliferation
B0042593biological_processglucose homeostasis
B0042802molecular_functionidentical protein binding
B0046203biological_processspermidine catabolic process
B0051604biological_processprotein maturation
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006412biological_processtranslation
C0008216biological_processspermidine metabolic process
C0008284biological_processpositive regulation of cell population proliferation
C0008612biological_processpeptidyl-lysine modification to peptidyl-hypusine
C0016740molecular_functiontransferase activity
C0034038molecular_functiondeoxyhypusine synthase activity
C0042102biological_processpositive regulation of T cell proliferation
C0042593biological_processglucose homeostasis
C0042802molecular_functionidentical protein binding
C0046203biological_processspermidine catabolic process
C0051604biological_processprotein maturation
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006412biological_processtranslation
D0008216biological_processspermidine metabolic process
D0008284biological_processpositive regulation of cell population proliferation
D0008612biological_processpeptidyl-lysine modification to peptidyl-hypusine
D0016740molecular_functiontransferase activity
D0034038molecular_functiondeoxyhypusine synthase activity
D0042102biological_processpositive regulation of T cell proliferation
D0042593biological_processglucose homeostasis
D0042802molecular_functionidentical protein binding
D0046203biological_processspermidine catabolic process
D0051604biological_processprotein maturation
E0003723molecular_functionRNA binding
E0003746molecular_functiontranslation elongation factor activity
E0005515molecular_functionprotein binding
E0005634cellular_componentnucleus
E0005642cellular_componentannulate lamellae
E0005643cellular_componentnuclear pore
E0005737cellular_componentcytoplasm
E0005789cellular_componentendoplasmic reticulum membrane
E0005829cellular_componentcytosol
E0006412biological_processtranslation
E0006414biological_processtranslational elongation
E0016020cellular_componentmembrane
E0017070molecular_functionU6 snRNA binding
E0033209biological_processtumor necrosis factor-mediated signaling pathway
E0043022molecular_functionribosome binding
E0043065biological_processpositive regulation of apoptotic process
E0045202cellular_componentsynapse
E0045901biological_processpositive regulation of translational elongation
E0045905biological_processpositive regulation of translational termination
E0045944biological_processpositive regulation of transcription by RNA polymerase II
E0098586biological_processcellular response to virus
E1902255biological_processpositive regulation of intrinsic apoptotic signaling pathway by p53 class mediator
Functional Information from PROSITE/UniProt
site_idPS00302
Number of Residues8
DetailsIF5A_HYPUSINE Eukaryotic initiation factor 5A hypusine signature. TGKHGhAK
ChainResidueDetails
ETHR48-LYS55

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"9405486","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues44
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9493264","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues44
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17525332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues70
DetailsRegion: {"description":"Interaction with DOHH","evidences":[{"source":"PubMed","id":"17213197","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19379712","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Hypusine","evidences":[{"source":"PubMed","id":"27306458","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3095320","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P63242","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 687
ChainResidueDetails
CGLU137electrostatic stabiliser
CASN292proton acceptor, proton donor
CASP333covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor

site_idMCSA2
Number of Residues3
DetailsM-CSA 687
ChainResidueDetails
DGLU137electrostatic stabiliser
DASN292proton acceptor, proton donor
DASP333covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor

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PDB entries from 2025-10-15

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