SAXSdb — 1rrp

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1. Protein Identity and Related Structures Protein Identity & Related Structures

RAN

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	NUCLEAR PORE COMPLEX PROTEIN NUP358 × 1 （P49792） MAGNESIUM ION × 1 PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	NUCLEAR PORE COMPLEX PROTEIN NUP358 × 1 （P49792） MAGNESIUM ION × 1 PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 water × 2	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 8	NUCLEAR PORE COMPLEX PROTEIN NUP358 × 4 （P49792） MAGNESIUM ION × 4 PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 4 water × 8	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 4	NUCLEAR PORE COMPLEX PROTEIN NUP358 × 2 （P49792） MAGNESIUM ION × 2 PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 2 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	RAN_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–204； UniProt 8–211 Author chain C； PDBConstruct 1–204； UniProt 8–211

NUCLEAR PORE COMPLEX PROTEIN NUP358

Homo sapiens

UniProt P49792

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	RAN × 1 （P62826） MAGNESIUM ION × 1 PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	RAN × 1 （P62826） MAGNESIUM ION × 1 PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 water × 2	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 8	RAN × 4 （P62826） MAGNESIUM ION × 4 PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 4 water × 8	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 4	RAN × 2 （P62826） MAGNESIUM ION × 2 PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 2 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	RBP2_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–134； UniProt 1171–1304 Author chain D； PDBConstruct 1–134； UniProt 1171–1304

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1rrp
Deposition date deposition_date	1999-01-15
Structure title title	STRUCTURE OF THE RAN-GPPNHP-RANBD1 COMPLEX
Keywords keywords	COMPLEX (SMALL GTPASE-NUCLEAR PROTEIN), SMALL GTPASE, NUCLEAR TRANSPORT, COMPLEX (SMALL GTPASE-NUCLEAR PROTEIN) complex; COMPLEX (SMALL GTPASE/NUCLEAR PROTEIN)
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1rrp__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1rrp__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1rrp__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	22.57 Å
Rg (electron density)	21.82 Å
Total Rg	22.65 Å
Atom count	2774
Residues	338
Excluded volume	49548 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1rrp__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1rrp__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`1rrp__assembly_3__model_1`	octameric （8）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`1rrp__assembly_4__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	RAN
Molecular weight formula_weight	23183.8 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C
Atom count atom_count	5402

QVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLEVAQTTALPD

Source Source

Source organism organism	Homo sapiens
Common name common_name	human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli BL21

Entity 2 Entity 2 polymer

Description description	NUCLEAR PORE COMPLEX PROTEIN NUP358
Molecular weight formula_weight	15703.0 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D

HFEPVVPLPDKIEVKTGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFVWHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQSI

Source Source

Source organism organism	Homo sapiens
Common name common_name	human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli BL21

Entity 3 Entity 3 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
Molecular weight formula_weight	522.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	36

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6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1rrpa_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.8 — G proteins

Domain ID domain_id	d1rrpb_
Class class	b — All beta proteins
Fold Fold fold	b.55 — PH domain-like barrel
Superfamily Superfamily superfamily	b.55.1 — PH domain-like
Family Family family	b.55.1.3 — Ran-binding domain

Domain ID domain_id	d1rrpc_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.8 — G proteins

Domain ID domain_id	d1rrpd_
Class class	b — All beta proteins
Fold Fold fold	b.55 — PH domain-like barrel
Superfamily Superfamily superfamily	b.55.1 — PH domain-like
Family Family family	b.55.1.3 — Ran-binding domain

CATH v4.4 (4 domains)

Domain ID domain_id	1rrpA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	1rrpB00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	29 — PH-domain like
Homologous superfamily homologous superfamily	30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

Domain ID domain_id	1rrpC00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	1rrpD00
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	29 — PH-domain like
Homologous superfamily homologous superfamily	30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

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7. Citations (7)

Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport.

Nature (1999)

PMID: 10078529 · DOI: 10.1038/17969 PRIMARY

Ranbp1 is Crucial for the Release of Rangtp from Importin Beta-Related Nuclear Transport Factors

FEBS Lett. (1997)

Dynamic and Equilibrium Studies on the Interaction of Ran with its Effector, Ranbp1

Biochemistry (1997)

A Ran-Binding Motif Found in Nuclear Pore Proteins

Trends Cell Biol. (1995)

A Giant Nucleopore Protein that Binds Ran/Tc4

Nature (1995)

;The C Terminus of the Nuclear Ran/Tc4 Gtpase Stabilizes the Gdp-Bound State and Mediates Interactions with Rcc1, Ran-Gap, and Htf9A/Ranbp1 ;

J.Biol.Chem. (1995)

Co-Activation of Rangtpase and Inhibition of GTP Dissociation by Ran-GTP Binding Protein Ranbp1

Embo J. (1995)

Unit-cell length a length_a	121.339 Å
Unit-cell length b length_b	139.463 Å
Unit-cell length c length_c	91.654 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	135.78 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.960 Å
Low-resolution limit resolution_low	12.500 Å
R factor r_factor	0.2520
R_work r_work	0.2520
R_free r_free	0.3040

STRUCTURE OF THE RAN-GPPNHP-RANBD1 COMPLEX

1. Protein Identity and Related Structures Protein Identity & Related Structures

RAN

State in the Current Structure

Other States of the Same Protein in the Database

NUCLEAR PORE COMPLEX PROTEIN NUP358

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1rrp__assembly_1__model_1

1rrp__assembly_1__model_1 | I(q)

1rrp__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (7)

STRUCTURE OF THE RAN-GPPNHP-RANBD1 COMPLEX

1. Protein Identity and Related Structures Protein Identity & Related Structures

RAN

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

NUCLEAR PORE COMPLEX PROTEIN NUP358

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1rrp__assembly_1__model_1

1rrp__assembly_1__model_1 | I(q)

1rrp__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (7)