8A0E

CryoEM structure of DHS-eIF5A1 complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006412	biological_process	translation
A	0008216	biological_process	spermidine metabolic process
A	0008284	biological_process	positive regulation of cell population proliferation
A	0008612	biological_process	peptidyl-lysine modification to peptidyl-hypusine
A	0016740	molecular_function	transferase activity
A	0034038	molecular_function	deoxyhypusine synthase activity
A	0042802	molecular_function	identical protein binding
A	0046203	biological_process	spermidine catabolic process
A	0051604	biological_process	protein maturation
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006412	biological_process	translation
B	0008216	biological_process	spermidine metabolic process
B	0008284	biological_process	positive regulation of cell population proliferation
B	0008612	biological_process	peptidyl-lysine modification to peptidyl-hypusine
B	0016740	molecular_function	transferase activity
B	0034038	molecular_function	deoxyhypusine synthase activity
B	0042802	molecular_function	identical protein binding
B	0046203	biological_process	spermidine catabolic process
B	0051604	biological_process	protein maturation
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006412	biological_process	translation
C	0008216	biological_process	spermidine metabolic process
C	0008284	biological_process	positive regulation of cell population proliferation
C	0008612	biological_process	peptidyl-lysine modification to peptidyl-hypusine
C	0016740	molecular_function	transferase activity
C	0034038	molecular_function	deoxyhypusine synthase activity
C	0042802	molecular_function	identical protein binding
C	0046203	biological_process	spermidine catabolic process
C	0051604	biological_process	protein maturation
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006412	biological_process	translation
D	0008216	biological_process	spermidine metabolic process
D	0008284	biological_process	positive regulation of cell population proliferation
D	0008612	biological_process	peptidyl-lysine modification to peptidyl-hypusine
D	0016740	molecular_function	transferase activity
D	0034038	molecular_function	deoxyhypusine synthase activity
D	0042802	molecular_function	identical protein binding
D	0046203	biological_process	spermidine catabolic process
D	0051604	biological_process	protein maturation
E	0003723	molecular_function	RNA binding
E	0003746	molecular_function	translation elongation factor activity
E	0005515	molecular_function	protein binding
E	0005634	cellular_component	nucleus
E	0005642	cellular_component	annulate lamellae
E	0005643	cellular_component	nuclear pore
E	0005654	cellular_component	nucleoplasm
E	0005737	cellular_component	cytoplasm
E	0005789	cellular_component	endoplasmic reticulum membrane
E	0005829	cellular_component	cytosol
E	0006412	biological_process	translation
E	0006414	biological_process	translational elongation
E	0016020	cellular_component	membrane
E	0017070	molecular_function	U6 snRNA binding
E	0033209	biological_process	tumor necrosis factor-mediated signaling pathway
E	0043022	molecular_function	ribosome binding
E	0045202	cellular_component	synapse
E	0045901	biological_process	positive regulation of translational elongation
E	0045944	biological_process	positive regulation of transcription by RNA polymerase II
E	0098586	biological_process	cellular response to virus
E	1902255	biological_process	positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator

Functional Information from PROSITE/UniProt

site_id	PS00302
Number of Residues	8
Details	IF5A_HYPUSINE Eukaryotic initiation factor 5A hypusine signature. TGKHGhAK

Chain	Residue	Details
E	THR48-LYS55

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"9405486","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	44
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9493264","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	44
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17525332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	70
Details	Region: {"description":"Interaction with DOHH","evidences":[{"source":"PubMed","id":"17213197","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19379712","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Hypusine","evidences":[{"source":"PubMed","id":"27306458","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3095320","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P63242","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 687

Chain	Residue	Details
C	GLU137	electrostatic stabiliser
C	ASN292	proton acceptor, proton donor
C	ASP333	covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor

---

site_id	MCSA2
Number of Residues	3
Details	M-CSA 687

Chain	Residue	Details
D	GLU137	electrostatic stabiliser
D	ASN292	proton acceptor, proton donor
D	ASP333	covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor

---