SAXSdb — 2wbl

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

RHO OF PLANTS GUANINE NUCLEOTIDE EXCHANGE FACTOR 8

ARABIDOPSIS THALIANA

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	RAC-LIKE GTP-BINDING PROTEIN ARAC2 × 2 （Q38903）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9LV40_ARATH
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–365； UniProt 76–440 Author chain B； PDBConstruct 1–365； UniProt 76–440

RAC-LIKE GTP-BINDING PROTEIN ARAC2

ARABIDOPSIS THALIANA

UniProt Q38903

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	RHO OF PLANTS GUANINE NUCLEOTIDE EXCHANGE FACTOR 8 × 2 （Q9LV40）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	RAC2_ARATH
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–180； UniProt 1–180 Author chain D； PDBConstruct 1–180； UniProt 1–180

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	2wbl
Deposition date deposition_date	2009-03-02
Structure title title	Three-dimensional structure of a binary ROP-PRONE complex
Keywords keywords	;MEMBRANE, PRENYLATION, METHYLATION, NUCLEOTIDE- BINDING, SIGNALING PROTEIN, NUCLEOTIDE-BINDING, COMPLEX OF PRONE-GEF WITH ROP SUBSTRATE, LIPOPROTEIN, GTP-BINDING ;; SIGNALING 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.

2wbl__assembly_1__model_1

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

Download this curve (.dat)

2wbl__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2wbl__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	34.39 Å
Rg (electron density)	33.86 Å
Total Rg	34.17 Å
Atom count	7497
Residues	995
Excluded volume	133650 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2wbl__assembly_1__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 (2)

Entity 1 Entity 1 polymer

Description description	RHO OF PLANTS GUANINE NUCLEOTIDE EXCHANGE FACTOR 8
Molecular weight formula_weight	41516.4 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	7497

GKRSERQQADMEMMKDRFAKLLLGEDMSGGGKGVSSALALSNAITNLAASIFGEQTKLQPMPQDRQARWKKEIDWLLSVTDHIVEFVPSQQTSKDGVCTEIMVTRQRGDLLMNIPALRKLDAMLIDTLDNFRGHNEFWYVSRDSEEGQQARNDRTNDKWWLPPVKVPPGGLSEPSRRMLYFQKDSVTQVQKAAMAINAQVLSEMEIPESYIDSLPKNGRASLGDSIYKSITEEWFDPEQFLAMLDMSTEHKVLDLKNRIEASVVIWKRKLHTKDTKSSWGSAVSLEKRELFEERAETILVLLKQKFPGLPQSSLDISKIQFNKDVGQAVLESYSRILESLAYTVMSRIEDVLYTDTLALKQTLLA

Source Source

Source organism organism	ARABIDOPSIS THALIANA
Common name common_name	MOUSE-EAR CRESS
NCBI taxonomy ID ncbi_taxonomy_id	3702
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	RAC-LIKE GTP-BINDING PROTEIN ARAC2
Molecular weight formula_weight	19873.8 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

MSTARFIKCVTVGDGAVGKTCMLISYTGNTFPTDYVPTVFDNFSANVVVDGSTVNLGLWDTAGQEDYNRLRPLSYRGADVFLLAFSLISKASYENIHKKWLPELKHYAPGIPIVLVGTKLDLRDDKQFLKDHPGAASITTAQGEELRKMIGAVRYLECSSKTQQNVKAVFDTAIRVALRP

Source Source

Source organism organism	ARABIDOPSIS THALIANA
Common name common_name	MOUSE-EAR CRESS
NCBI taxonomy ID ncbi_taxonomy_id	3702
Host organism host_organism	ESCHERICHIA COLI

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6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d2wblc_
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	d2wbld_
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

CATH v4.4 (6 domains)

Domain ID domain_id	2wblA01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	2010 — PRONE domain, subdomain 1

Domain ID domain_id	2wblA02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	1310 — PRONE domain, subdomain 2

Domain ID domain_id	2wblB01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	2010 — PRONE domain, subdomain 1

Domain ID domain_id	2wblB02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	1310 — PRONE domain, subdomain 2

Domain ID domain_id	2wblC00
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	2wblD00
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

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Unit-cell length a length_a	80.550 Å
Unit-cell length b length_b	110.220 Å
Unit-cell length c length_c	151.980 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.900 Å
Low-resolution limit resolution_low	49.410 Å
R factor r_factor	0.2170
R_work r_work	0.2150
R_free r_free	0.2610

Three-dimensional structure of a binary ROP-PRONE complex

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

RHO OF PLANTS GUANINE NUCLEOTIDE EXCHANGE FACTOR 8

State in the Current Structure

Other States of the Same Protein in the Database

RAC-LIKE GTP-BINDING PROTEIN ARAC2

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

2wbl__assembly_1__model_1

2wbl__assembly_1__model_1 | I(q)

2wbl__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (2 domains)

CATH v4.4 (6 domains)

7. Citations (2)

Three-dimensional structure of a binary ROP-PRONE complex

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

RHO OF PLANTS GUANINE NUCLEOTIDE EXCHANGE FACTOR 8

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

RAC-LIKE GTP-BINDING PROTEIN ARAC2

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

2wbl__assembly_1__model_1

2wbl__assembly_1__model_1 | I(q)

2wbl__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (2 domains)

CATH v4.4 (6 domains)

7. Citations (2)