Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6Q84

Crystal structure of RanGTP-Pdr6-eIF5A export complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005049	molecular_function	nuclear export signal receptor activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005635	cellular_component	nuclear envelope
A	0005737	cellular_component	cytoplasm
A	0006606	biological_process	protein import into nucleus
A	0008361	biological_process	regulation of cell size
A	0051168	biological_process	nuclear export
A	0061608	molecular_function	nuclear import signal receptor activity
B	0003924	molecular_function	GTPase activity
B	0005525	molecular_function	GTP binding
B	0006913	biological_process	nucleocytoplasmic transport
C	0002182	biological_process	cytoplasmic translational elongation
C	0002184	biological_process	cytoplasmic translational termination
C	0003723	molecular_function	RNA binding
C	0003743	molecular_function	translation initiation factor activity
C	0003746	molecular_function	translation elongation factor activity
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0005829	cellular_component	cytosol
C	0006412	biological_process	translation
C	0006413	biological_process	translational initiation
C	0006414	biological_process	translational elongation
C	0006452	biological_process	translational frameshifting
C	0043022	molecular_function	ribosome binding
C	0045901	biological_process	positive regulation of translational elongation
C	0045905	biological_process	positive regulation of translational termination
C	0045948	biological_process	positive regulation of translational initiation
C	0048471	cellular_component	perinuclear region of cytoplasm
C	0072344	biological_process	rescue of stalled ribosome
C	0097622	biological_process	cytoplasmic translational elongation through polyproline stretches
C	0140708	biological_process	CAT tailing
C	1903272	biological_process	positive regulation of cytoplasmic translational elongation through polyproline stretches
D	0005049	molecular_function	nuclear export signal receptor activity
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005635	cellular_component	nuclear envelope
D	0005737	cellular_component	cytoplasm
D	0006606	biological_process	protein import into nucleus
D	0008361	biological_process	regulation of cell size
D	0051168	biological_process	nuclear export
D	0061608	molecular_function	nuclear import signal receptor activity
E	0003924	molecular_function	GTPase activity
E	0005525	molecular_function	GTP binding
E	0006913	biological_process	nucleocytoplasmic transport
F	0002182	biological_process	cytoplasmic translational elongation
F	0002184	biological_process	cytoplasmic translational termination
F	0003723	molecular_function	RNA binding
F	0003743	molecular_function	translation initiation factor activity
F	0003746	molecular_function	translation elongation factor activity
F	0005515	molecular_function	protein binding
F	0005737	cellular_component	cytoplasm
F	0005739	cellular_component	mitochondrion
F	0005829	cellular_component	cytosol
F	0006412	biological_process	translation
F	0006413	biological_process	translational initiation
F	0006414	biological_process	translational elongation
F	0006452	biological_process	translational frameshifting
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	0045948	biological_process	positive regulation of translational initiation
F	0048471	cellular_component	perinuclear region of cytoplasm
F	0072344	biological_process	rescue of stalled ribosome
F	0097622	biological_process	cytoplasmic translational elongation through polyproline stretches
F	0140708	biological_process	CAT tailing
F	1903272	biological_process	positive regulation of cytoplasmic translational elongation through polyproline stretches

Functional Information from PDB Data

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

Chain	Residue
B	GLY19
B	LYS37
B	LYS38
B	TYR39
B	VAL40
B	ALA41
B	THR42
B	THR66
B	ASN122
B	LYS123
B	ASP125
B	GLY20
B	ILE126
B	SER150
B	ALA151
B	LYS152
B	MG218
B	THR21
B	GLY22
B	LYS23
B	THR24
B	THR25
B	PHE35
B	GLU36

site_id	AC2
Number of Residues	4
Details	binding site for residue MG B 218

Chain	Residue
B	THR24
B	THR42
B	ASP65
B	GTP217

site_id	AC3
Number of Residues	28
Details	binding site for residue GTP E 217

Chain	Residue
E	ASP18
E	GLY19
E	GLY20
E	THR21
E	GLY22
E	LYS23
E	THR24
E	THR25
E	PHE35
E	GLU36
E	LYS37
E	LYS38
E	TYR39
E	VAL40
E	ALA41
E	THR42
E	THR66
E	ALA67
E	GLY68
E	LEU69
E	ASN122
E	LYS123
E	ASP125
E	ILE126
E	SER150
E	ALA151
E	LYS152
E	MG218

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

Chain	Residue
E	THR24
E	THR42
E	ASP65
E	THR66
E	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
C	THR49-LYS56

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: Hypusine => ECO:0000269\|PubMed:19120453, ECO:0000269\|PubMed:26715760, ECO:0000269\|PubMed:27196944, ECO:0007744\|PDB:5DC3, ECO:0007744\|PDB:5GAK

Chain	Residue	Details
C	LYS51
F	LYS51

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:17330950, ECO:0007744\|PubMed:18407956

Chain	Residue	Details
C	SER74
F	SER74

site_id	SWS_FT_FI3
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744\|PubMed:22106047

Chain	Residue	Details
C	LYS86
E	GLY68
F	LYS86

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
B	ASN122
E	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
B	SER150
E	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
B	LEU69
E	LEU69

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

Chain	Residue	Details
B	THR24
E	THR24

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

Chain	Residue	Details
B	LYS37
E	LYS37

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

Chain	Residue	Details
B	LYS60
B	LYS99
E	LYS60
E	LYS99

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

Chain	Residue	Details
B	LYS71
E	LYS71

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

Chain	Residue	Details
B	LYS134
E	LYS134

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

Chain	Residue	Details
B	LYS159
E	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
B	LYS71
E	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
B	LYS152
E	LYS152

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