Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5DLQ

Crystal structure of RanGTP-Exportin 4-eIF5A complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005049	molecular_function	nuclear export signal receptor activity
A	0005634	cellular_component	nucleus
A	0005643	cellular_component	nuclear pore
A	0005737	cellular_component	cytoplasm
A	0006611	biological_process	protein export from nucleus
A	0015031	biological_process	protein transport
A	0051169	biological_process	nuclear transport
B	0005049	molecular_function	nuclear export signal receptor activity
B	0005634	cellular_component	nucleus
B	0005643	cellular_component	nuclear pore
B	0005737	cellular_component	cytoplasm
B	0006611	biological_process	protein export from nucleus
B	0015031	biological_process	protein transport
B	0051169	biological_process	nuclear transport
C	0003924	molecular_function	GTPase activity
C	0005525	molecular_function	GTP binding
C	0006913	biological_process	nucleocytoplasmic transport
D	0003924	molecular_function	GTPase activity
D	0005525	molecular_function	GTP binding
D	0006913	biological_process	nucleocytoplasmic transport
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	0005737	cellular_component	cytoplasm
E	0005783	cellular_component	endoplasmic reticulum
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	0045901	biological_process	positive regulation of translational elongation
E	0045905	biological_process	positive regulation of translational termination
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
F	0003723	molecular_function	RNA binding
F	0003746	molecular_function	translation elongation factor activity
F	0005515	molecular_function	protein binding
F	0005634	cellular_component	nucleus
F	0005642	cellular_component	annulate lamellae
F	0005643	cellular_component	nuclear pore
F	0005737	cellular_component	cytoplasm
F	0005783	cellular_component	endoplasmic reticulum
F	0005789	cellular_component	endoplasmic reticulum membrane
F	0005829	cellular_component	cytosol
F	0006412	biological_process	translation
F	0006414	biological_process	translational elongation
F	0016020	cellular_component	membrane
F	0017070	molecular_function	U6 snRNA binding
F	0033209	biological_process	tumor necrosis factor-mediated signaling pathway
F	0043022	molecular_function	ribosome binding
F	0045901	biological_process	positive regulation of translational elongation
F	0045905	biological_process	positive regulation of translational termination
F	0045944	biological_process	positive regulation of transcription by RNA polymerase II
F	0098586	biological_process	cellular response to virus
F	1902255	biological_process	positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator

Functional Information from PDB Data

site_id	AC1
Number of Residues	24
Details	binding site for residue GTP C 217

Chain	Residue
B	PRO974
C	LYS37
C	TYR39
C	ALA41
C	THR42
C	ALA67
C	GLY68
C	LEU69
C	ASN122
C	LYS123
C	ASP125
C	GLY19
C	ILE126
C	SER150
C	ALA151
C	LYS152
C	MG218
C	GLY20
C	GLY22
C	LYS23
C	THR24
C	THR25
C	PHE35
C	GLU36

site_id	AC2
Number of Residues	6
Details	binding site for residue MG C 218

Chain	Residue
C	LYS23
C	THR24
C	THR42
C	ASP65
C	THR66
C	GTP217

site_id	AC3
Number of Residues	24
Details	binding site for residue GTP D 217

Chain	Residue
A	PRO974
D	GLY19
D	GLY20
D	THR21
D	GLY22
D	LYS23
D	THR24
D	THR25
D	PHE35
D	GLU36
D	LYS37
D	TYR39
D	ALA41
D	THR42
D	ALA67
D	GLY68
D	ASN122
D	LYS123
D	ASP125
D	ILE126
D	SER150
D	ALA151
D	LYS152
D	MG218

site_id	AC4
Number of Residues	5
Details	binding site for residue MG D 218

Chain	Residue
D	LYS23
D	THR24
D	THR42
D	ASP65
D	GTP217

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
F	THR48-LYS55

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000269\|PubMed:19379712

Chain	Residue	Details
F	THR17
E	THR17
A	LEU484
A	TRP541

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: Hypusine => ECO:0000269\|PubMed:27306458, ECO:0000269\|PubMed:3095320

Chain	Residue	Details
F	MET20
E	MET20

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P63242

Chain	Residue	Details
E	LEU91
F	LEU91

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:10078529, ECO:0000269\|PubMed:10353245, ECO:0000269\|PubMed:10367892, ECO:0000269\|PubMed:11832950, ECO:0000269\|PubMed:18611384, ECO:0000269\|PubMed:19389996, ECO:0000269\|PubMed:19505478, ECO:0000269\|PubMed:24449914, ECO:0000269\|PubMed:24915079, ECO:0000269\|PubMed:26272610, ECO:0000269\|PubMed:26349033, ECO:0000269\|PubMed:28282025, ECO:0000269\|PubMed:7885480, ECO:0007744\|PDB:1IBR, ECO:0007744\|PDB:1K5D, ECO:0007744\|PDB:1QBK, ECO:0007744\|PDB:1RRP, ECO:0007744\|PDB:3CH5, ECO:0007744\|PDB:3GJ0, ECO:0007744\|PDB:3GJ3, ECO:0007744\|PDB:3GJ4, ECO:0007744\|PDB:3GJ5, ECO:0007744\|PDB:3GJ6, ECO:0007744\|PDB:3GJ7, ECO:0007744\|PDB:3GJ8, ECO:0007744\|PDB:3GJX, ECO:0007744\|PDB:3NBY, ECO:0007744\|PDB:3NBZ, ECO:0007744\|PDB:3NC0, ECO:0007744\|PDB:3NC1, ECO:0007744\|PDB:3ZJY, ECO:0007744\|PDB:4C0Q, ECO:0007744\|PDB:4OL0, ECO:0007744\|PDB:5CIQ, ECO:0007744\|PDB:5CIT, ECO:0007744\|PDB:5CIW, ECO:0007744\|PDB:5CJ2, ECO:0007744\|PDB:5CLL, ECO:0007744\|PDB:5DH9, ECO:0007744\|PDB:5DHA, ECO:0007744\|PDB:5DHF, ECO:0007744\|PDB:5DI9, ECO:0007744\|PDB:5DIF, ECO:0007744\|PDB:5DIS, ECO:0007744\|PDB:5DLQ, ECO:0007744\|PDB:5JLJ, ECO:0007744\|PDB:5UWH, ECO:0007744\|PDB:5UWI, ECO:0007744\|PDB:5UWJ, ECO:0007744\|PDB:5UWO, ECO:0007744\|PDB:5UWP, ECO:0007744\|PDB:5UWQ, ECO:0007744\|PDB:5UWR, ECO:0007744\|PDB:5UWS, ECO:0007744\|PDB:5UWT, ECO:0007744\|PDB:5UWU, ECO:0007744\|PDB:5UWW

Chain	Residue	Details
D	ASN122
C	ASN122

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:10078529, ECO:0000269\|PubMed:10353245, ECO:0000269\|PubMed:10367892, ECO:0000269\|PubMed:11832950, ECO:0000269\|PubMed:18611384, ECO:0000269\|PubMed:19389996, ECO:0000269\|PubMed:19505478, ECO:0000269\|PubMed:24449914, ECO:0000269\|PubMed:24915079, ECO:0000269\|PubMed:26272610, ECO:0000269\|PubMed:26349033, ECO:0000269\|PubMed:28282025, ECO:0000269\|PubMed:7885480, ECO:0007744\|PDB:1K5G, ECO:0007744\|PDB:3CH5, ECO:0007744\|PDB:3GJ0, ECO:0007744\|PDB:3GJ3, ECO:0007744\|PDB:3GJ4, ECO:0007744\|PDB:3GJ5, ECO:0007744\|PDB:3GJ6, ECO:0007744\|PDB:3GJ7, ECO:0007744\|PDB:3GJ8, ECO:0007744\|PDB:3GJX, ECO:0007744\|PDB:3NBY, ECO:0007744\|PDB:3NBZ, ECO:0007744\|PDB:3NC0, ECO:0007744\|PDB:3NC1, ECO:0007744\|PDB:3ZJY, ECO:0007744\|PDB:4C0Q, ECO:0007744\|PDB:4OL0, ECO:0007744\|PDB:5CIQ, ECO:0007744\|PDB:5CIT, ECO:0007744\|PDB:5CIW, ECO:0007744\|PDB:5CJ2, ECO:0007744\|PDB:5CLL, ECO:0007744\|PDB:5CLQ, ECO:0007744\|PDB:5DH9, ECO:0007744\|PDB:5DHA, ECO:0007744\|PDB:5DHF, ECO:0007744\|PDB:5DI9, ECO:0007744\|PDB:5DIF, ECO:0007744\|PDB:5DIS, ECO:0007744\|PDB:5DLQ, ECO:0007744\|PDB:5JLJ, ECO:0007744\|PDB:5UWH, ECO:0007744\|PDB:5UWI, ECO:0007744\|PDB:5UWJ, ECO:0007744\|PDB:5UWO, ECO:0007744\|PDB:5UWP, ECO:0007744\|PDB:5UWQ, ECO:0007744\|PDB:5UWR, ECO:0007744\|PDB:5UWS, ECO:0007744\|PDB:5UWT, ECO:0007744\|PDB:5UWU, ECO:0007744\|PDB:5UWW

Chain	Residue	Details
D	SER150
C	SER150

site_id	SWS_FT_FI6
Number of Residues	2
Details	SITE: Essential for GTP hydrolysis => ECO:0000269\|PubMed:18591255, ECO:0000269\|PubMed:26272610, ECO:0000269\|PubMed:8636225

Chain	Residue	Details
C	LEU69
D	LEU69

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
C	THR24
D	THR24

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000269\|PubMed:31075303

Chain	Residue	Details
C	LYS37
D	LYS37

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
C	LYS60
D	LYS60
C	LYS99
D	LYS99

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: N6-acetyllysine; alternate => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
C	LYS71
D	LYS71

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000269\|PubMed:29040603

Chain	Residue	Details
C	LYS134
D	LYS134

site_id	SWS_FT_FI12
Number of Residues	2
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:P62827

Chain	Residue	Details
C	LYS159
D	LYS159

site_id	SWS_FT_FI13
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate

Chain	Residue	Details
C	LYS71
D	LYS71

site_id	SWS_FT_FI14
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744\|PubMed:28112733

Chain	Residue	Details
C	LYS152
D	LYS152

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)