Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3GJ8

Crystal structure of human RanGDP-Nup153ZnF34 complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000054	biological_process	ribosomal subunit export from nucleus
A	0000055	biological_process	ribosomal large subunit export from nucleus
A	0000056	biological_process	ribosomal small subunit export from nucleus
A	0000070	biological_process	mitotic sister chromatid segregation
A	0000166	molecular_function	nucleotide binding
A	0000278	biological_process	mitotic cell cycle
A	0000287	molecular_function	magnesium ion binding
A	0000785	cellular_component	chromatin
A	0001673	cellular_component	male germ cell nucleus
A	0002177	cellular_component	manchette
A	0003682	molecular_function	chromatin binding
A	0003723	molecular_function	RNA binding
A	0003924	molecular_function	GTPase activity
A	0003925	molecular_function	G protein activity
A	0005049	molecular_function	nuclear export signal receptor activity
A	0005515	molecular_function	protein binding
A	0005525	molecular_function	GTP binding
A	0005634	cellular_component	nucleus
A	0005635	cellular_component	nuclear envelope
A	0005643	cellular_component	nuclear pore
A	0005654	cellular_component	nucleoplasm
A	0005730	cellular_component	nucleolus
A	0005737	cellular_component	cytoplasm
A	0005814	cellular_component	centriole
A	0005829	cellular_component	cytosol
A	0006259	biological_process	DNA metabolic process
A	0006606	biological_process	protein import into nucleus
A	0006611	biological_process	protein export from nucleus
A	0006913	biological_process	nucleocytoplasmic transport
A	0007049	biological_process	cell cycle
A	0007052	biological_process	mitotic spindle organization
A	0007286	biological_process	spermatid development
A	0008104	biological_process	protein localization
A	0014070	biological_process	response to organic cyclic compound
A	0015031	biological_process	protein transport
A	0016020	cellular_component	membrane
A	0016032	biological_process	viral process
A	0016787	molecular_function	hydrolase activity
A	0019003	molecular_function	GDP binding
A	0019904	molecular_function	protein domain specific binding
A	0021766	biological_process	hippocampus development
A	0030036	biological_process	actin cytoskeleton organization
A	0030496	cellular_component	midbody
A	0031503	biological_process	protein-containing complex localization
A	0032092	biological_process	positive regulation of protein binding
A	0032991	cellular_component	protein-containing complex
A	0035281	biological_process	pre-miRNA export from nucleus
A	0036126	cellular_component	sperm flagellum
A	0042307	biological_process	positive regulation of protein import into nucleus
A	0042470	cellular_component	melanosome
A	0042565	cellular_component	RNA nuclear export complex
A	0044877	molecular_function	protein-containing complex binding
A	0045296	molecular_function	cadherin binding
A	0045505	molecular_function	dynein intermediate chain binding
A	0046039	biological_process	GTP metabolic process
A	0046872	molecular_function	metal ion binding
A	0046982	molecular_function	protein heterodimerization activity
A	0051301	biological_process	cell division
A	0055037	cellular_component	recycling endosome
A	0061015	biological_process	snRNA import into nucleus
A	0061676	molecular_function	importin-alpha family protein binding
A	0070062	cellular_component	extracellular exosome
A	0070883	molecular_function	pre-miRNA binding
A	0071389	biological_process	cellular response to mineralocorticoid stimulus
A	0090543	cellular_component	Flemming body
A	1902570	biological_process	protein localization to nucleolus
C	0000054	biological_process	ribosomal subunit export from nucleus
C	0000055	biological_process	ribosomal large subunit export from nucleus
C	0000056	biological_process	ribosomal small subunit export from nucleus
C	0000070	biological_process	mitotic sister chromatid segregation
C	0000166	molecular_function	nucleotide binding
C	0000278	biological_process	mitotic cell cycle
C	0000287	molecular_function	magnesium ion binding
C	0000785	cellular_component	chromatin
C	0001673	cellular_component	male germ cell nucleus
C	0002177	cellular_component	manchette
C	0003682	molecular_function	chromatin binding
C	0003723	molecular_function	RNA binding
C	0003924	molecular_function	GTPase activity
C	0003925	molecular_function	G protein activity
C	0005049	molecular_function	nuclear export signal receptor activity
C	0005515	molecular_function	protein binding
C	0005525	molecular_function	GTP binding
C	0005634	cellular_component	nucleus
C	0005635	cellular_component	nuclear envelope
C	0005643	cellular_component	nuclear pore
C	0005654	cellular_component	nucleoplasm
C	0005730	cellular_component	nucleolus
C	0005737	cellular_component	cytoplasm
C	0005814	cellular_component	centriole
C	0005829	cellular_component	cytosol
C	0006259	biological_process	DNA metabolic process
C	0006606	biological_process	protein import into nucleus
C	0006611	biological_process	protein export from nucleus
C	0006913	biological_process	nucleocytoplasmic transport
C	0007049	biological_process	cell cycle
C	0007052	biological_process	mitotic spindle organization
C	0007286	biological_process	spermatid development
C	0008104	biological_process	protein localization
C	0014070	biological_process	response to organic cyclic compound
C	0015031	biological_process	protein transport
C	0016020	cellular_component	membrane
C	0016032	biological_process	viral process
C	0016787	molecular_function	hydrolase activity
C	0019003	molecular_function	GDP binding
C	0019904	molecular_function	protein domain specific binding
C	0021766	biological_process	hippocampus development
C	0030036	biological_process	actin cytoskeleton organization
C	0030496	cellular_component	midbody
C	0031503	biological_process	protein-containing complex localization
C	0032092	biological_process	positive regulation of protein binding
C	0032991	cellular_component	protein-containing complex
C	0035281	biological_process	pre-miRNA export from nucleus
C	0036126	cellular_component	sperm flagellum
C	0042307	biological_process	positive regulation of protein import into nucleus
C	0042470	cellular_component	melanosome
C	0042565	cellular_component	RNA nuclear export complex
C	0044877	molecular_function	protein-containing complex binding
C	0045296	molecular_function	cadherin binding
C	0045505	molecular_function	dynein intermediate chain binding
C	0046039	biological_process	GTP metabolic process
C	0046872	molecular_function	metal ion binding
C	0046982	molecular_function	protein heterodimerization activity
C	0051301	biological_process	cell division
C	0055037	cellular_component	recycling endosome
C	0061015	biological_process	snRNA import into nucleus
C	0061676	molecular_function	importin-alpha family protein binding
C	0070062	cellular_component	extracellular exosome
C	0070883	molecular_function	pre-miRNA binding
C	0071389	biological_process	cellular response to mineralocorticoid stimulus
C	0090543	cellular_component	Flemming body
C	1902570	biological_process	protein localization to nucleolus

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 301

Chain	Residue
A	THR24
A	GDP302
A	HOH479
A	HOH480
A	HOH481
A	HOH482

site_id	AC2
Number of Residues	23
Details	BINDING SITE FOR RESIDUE GDP A 302

Chain	Residue
A	LYS23
A	THR24
A	THR25
A	ASN122
A	LYS123
A	ASP125
A	ILE126
A	SER150
A	ALA151
A	LYS152
A	HOH240
A	HOH254
A	HOH279
A	MG301
A	HOH336
A	HOH350
A	HOH404
A	HOH417
A	HOH479
A	HOH482
A	GLY20
A	THR21
A	GLY22

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 303

Chain	Residue
A	PRO180
A	ALA181
A	HOH322
C	MG303

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 300

Chain	Residue
B	CYS852
B	CYS855
B	CYS866
B	CYS869

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 303

Chain	Residue
A	MG303
C	PRO180
C	ALA181
C	HOH243
C	HOH341

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 301

Chain	Residue
C	THR24
C	GDP302
C	HOH475
C	HOH476
C	HOH477
C	HOH478

site_id	AC7
Number of Residues	24
Details	BINDING SITE FOR RESIDUE GDP C 302

Chain	Residue
C	GLY20
C	THR21
C	GLY22
C	LYS23
C	THR24
C	THR25
C	ASN122
C	LYS123
C	ASP125
C	ILE126
C	SER150
C	ALA151
C	LYS152
C	HOH219
C	HOH249
C	HOH274
C	MG301
C	HOH310
C	HOH373
C	HOH476
C	HOH478
C	HOH499
C	HOH540
C	HOH541

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 300

Chain	Residue
D	CYS852
D	CYS855
D	CYS866
D	CYS869

Functional Information from PROSITE/UniProt

site_id	PS01358
Number of Residues	20
Details	ZF_RANBP2_1 Zinc finger RanBP2-type signature. WeCpv..CcvsNkaedsrCvsC

Chain	Residue	Details
B	TRP793-CYS812
B	TRP850-CYS869

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	58
Details	ZN_FING: RanBP2-type 4 => ECO:0000255\|PROSITE-ProRule:PRU00322

Chain	Residue	Details
B	PRO846-GLY875
D	PRO846-GLY875

site_id	SWS_FT_FI2
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269\|PubMed:18611384, ECO:0000269\|PubMed:19505478

Chain	Residue	Details
B	CYS795
D	CYS798
D	CYS809
D	CYS812
D	CYS852
D	CYS855
D	CYS866
D	CYS869
B	CYS798
B	CYS809
B	CYS812
B	CYS852
B	CYS855
B	CYS866
B	CYS869
D	CYS795

site_id	SWS_FT_FI3
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: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: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
A	GLY68
C	GLY68

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
A	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
A	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
A	GLN69
C	GLN69

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: N-acetylalanine => ECO:0000269\|Ref.12, ECO:0007744\|PubMed:19413330, ECO:0007744\|PubMed:22223895, ECO:0007744\|PubMed:22814378

Chain	Residue	Details
A	ALA2
C	ALA2

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	THR24
C	THR24

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000269\|PubMed:31075303

Chain	Residue	Details
A	LYS37
C	LYS37

site_id	SWS_FT_FI10
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
A	LYS60
A	LYS99
C	LYS60
C	LYS99

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: N6-acetyllysine; alternate => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
A	LYS71
C	LYS71

site_id	SWS_FT_FI12
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000269\|PubMed:29040603

Chain	Residue	Details
A	LYS134
C	LYS134

site_id	SWS_FT_FI13
Number of Residues	2
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:P62827

Chain	Residue	Details
A	LYS159
C	LYS159

site_id	SWS_FT_FI14
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate

Chain	Residue	Details
A	LYS71
C	LYS71

site_id	SWS_FT_FI15
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744\|PubMed:28112733

Chain	Residue	Details
A	LYS152
C	LYS152

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