SAXSdb — 1hh4

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

RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1

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	RHO GDP-DISSOCIATION INHIBITOR 1 × 1 （P52565） GUANOSINE-5'-DIPHOSPHATE × 1 MAGNESIUM ION × 1 GERAN-8-YL GERAN × 1 water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	RHO GDP-DISSOCIATION INHIBITOR 1 × 1 （P52565） GUANOSINE-5'-DIPHOSPHATE × 1 MAGNESIUM ION × 1 GERAN-8-YL GERAN × 1 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	RAC1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–192； UniProt 1–192 Author chain B； PDBConstruct 1–192； UniProt 1–192

RHO GDP-DISSOCIATION INHIBITOR 1

HOMO SAPIENS

UniProt P52565

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1 × 1 （P15154） GUANOSINE-5'-DIPHOSPHATE × 1 MAGNESIUM ION × 1 GERAN-8-YL GERAN × 1 water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1 × 1 （P15154） GUANOSINE-5'-DIPHOSPHATE × 1 MAGNESIUM ION × 1 GERAN-8-YL GERAN × 1 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	GDIR_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain D； PDBConstruct 1–204； UniProt 1–204 Author chain E； PDBConstruct 1–204； UniProt 1–204

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	1hh4
Deposition date deposition_date	2000-12-20
Structure title title	Rac1-RhoGDI complex involved in NADPH oxidase activation
Keywords keywords	;SIGNALING PROTEIN/INHIBITOR, SINGAL PROTEIN INHIBITOR COMPLEX, SMALL G PROTEIN, GTPASE ACTIVATION, GTP-BINDING, PRENYLATION, LIPOPROTEIN, SIGNALING PROTEIN-INHIBITOR complex ;; SIGNALING PROTEIN/INHIBITOR
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.

1hh4__assembly_1__model_1

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

Download this curve (.dat)

1hh4__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1hh4__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	24.13 Å
Rg (electron density)	23.27 Å
Total Rg	24.18 Å
Atom count	2942
Residues	375
Excluded volume	52590 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1hh4__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1hh4__assembly_2__model_1`	dimeric （2）	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 (6)

Entity 1 Entity 1 polymer

Description description	RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1
Molecular weight formula_weight	21383.9 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	5908

PQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTDVSLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLRDDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQRGLKTVFDEAIRAVLCPPPVKKRKRKCLLL

Source Source

Source organism organism	HOMO SAPIENS
Common name common_name	HUMAN
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	SPODOPTERA FRUGIPERDA

Entity 2 Entity 2 polymer

Description description	RHO GDP-DISSOCIATION INHIBITOR 1
Molecular weight formula_weight	23238.1 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

MAEQEPTAEQLAQIAAENEEDEHSVNYKPPAQKSIQEIQELDKDDESLRKYKEALLGRVAVSADPNVPNVVVTGLTLVCSSAPGPLELDLTGDLESFKKQSFVLKEGVEYRIKISFRVNREIVSGMKYIQHTYRKGVKIDKTDYMVGSYGPRAEEYEFLTPVEEAPKGMLARGSYSIKSRFTDDDKTDHLSWEWNLTIKKDWKD

Source Source

Source organism organism	HOMO SAPIENS
Common name common_name	HUMAN
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	SPODOPTERA FRUGIPERDA

Entity 3 Entity 3 non-polymer

Description description	GUANOSINE-5'-DIPHOSPHATE
Molecular weight formula_weight	443.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

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

Entity 5 Entity 5 non-polymer

Description description	GERAN-8-YL GERAN
Molecular weight formula_weight	274.5 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	30

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6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d1hh4a1
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	d1hh4a2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1hh4b1
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	d1hh4b2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1hh4d_
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.18 — E set domains
Family Family family	b.1.18.8 — RhoGDI-like

Domain ID domain_id	d1hh4e_
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.18 — E set domains
Family Family family	b.1.18.8 — RhoGDI-like

CATH v4.4 (4 domains)

Domain ID domain_id	1hh4A00
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	1hh4B00
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	1hh4D00
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	50 — Coagulation Factor XIII; Chain A, domain 1
Homologous superfamily homologous superfamily	30 — Coagulation Factor XIII, subunit A, domain 1

Domain ID domain_id	1hh4E00
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	50 — Coagulation Factor XIII; Chain A, domain 1
Homologous superfamily homologous superfamily	30 — Coagulation Factor XIII, subunit A, domain 1

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Unit-cell length a length_a	154.700 Å
Unit-cell length b length_b	88.700 Å
Unit-cell length c length_c	62.600 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 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	2.700 Å
Low-resolution limit resolution_low	19.800 Å
R factor r_factor	0.2560
R_work r_work	0.2560
R_free r_free	0.2800

Rac1-RhoGDI complex involved in NADPH oxidase activation

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

RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1

State in the Current Structure

Other States of the Same Protein in the Database

RHO GDP-DISSOCIATION INHIBITOR 1

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

1hh4__assembly_1__model_1

1hh4__assembly_1__model_1 | I(q)

1hh4__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 (6)

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 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (6 domains)

CATH v4.4 (4 domains)

7. Citations (1)

Rac1-RhoGDI complex involved in NADPH oxidase activation

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

RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

RHO GDP-DISSOCIATION INHIBITOR 1

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

1hh4__assembly_1__model_1

1hh4__assembly_1__model_1 | I(q)

1hh4__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 (6)

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 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (6 domains)

CATH v4.4 (4 domains)

7. Citations (1)