SAXSdb — 5cm8

▼

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

Ral guanine nucleotide dissociation stimulator-like 2

Mus musculus

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 protein Ral-a × 1 （P48555） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	RGL2_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 9–473； UniProt 50–514

Ras-related protein Ral-a

Drosophila melanogaster

UniProt P48555

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Ral guanine nucleotide dissociation stimulator-like 2 × 1 （Q61193） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	RALA_DROME
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 3–203； UniProt 1–201

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	5cm8
Deposition date deposition_date	2015-07-16
Structure title title	Structural Basis for the Selectivity of Guanine Nucleotide Exchange Factors for the small G-protein Ral
Keywords keywords	Complex G-protein Exchange Factor, signaling protein; SIGNALING PROTEIN
Experimental Method method	X-RAY DIFFRACTION

▼

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.

5cm8__assembly_1__model_1

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

Download this curve (.dat)

5cm8__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

5cm8__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	28.11 Å
Rg (electron density)	27.21 Å
Total Rg	27.96 Å
Atom count	4589
Residues	588
Excluded volume	81118 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`5cm8__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Ral guanine nucleotide dissociation stimulator-like 2
Molecular weight formula_weight	52113.9 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	4634

GPLGSPNSEEEASVSVWDEEEDGATFTVTSRQYRPLDPLAPLPPPRSSRRLRAGTLEALVRHLLDARTAGADMMFTPALLATHRAFTSTPALFGLVADRLEALESYPPGELERTTGVAISVLSTWLASHPEDFGSEVKGQLDRLESFLLRTGYAAREGVVGGSADLIRNLRARVDPRAPDLPKPLALPGDSPADPTDVLVFLADHLAEQLTLLDAELFLNLIPSQCLGGLWGHRDRPGHSHLCPSVRATVTQFNKVAGAVVSSVLGATSIGEGPREVTVRPLRPPQRARLLEKWIRVAEECRLLRNFSSVYAVVSALQSSPIHRLRAAWGETTRDSLRVFSSLCQIFSEEDNYSQSRELLTQEVKPQPPVEPHSKKAPRSGFRGGGVVPYLGTFLKDLVMLDAASKDELENGYINFDKRRKEFAILSELLRLQKECRGYDLRPNSDIQQWLQGLQPLTEAQSHRVSCEVEPPG

Source Source

Source organism organism	Mus musculus
Common name common_name	House Mouse
NCBI taxonomy ID ncbi_taxonomy_id	10090
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Ras-related protein Ral-a
Molecular weight formula_weight	23117.3 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

GSMSKKPTAGPALHKVIMVGSGGVGKSALTLQFMYDEFVEDYEPTKADSYRKKVVLDGEEVQIDILDTAGQEDYAAIRDNYFRSGEGFLCVFSITDDESFQATQEFREQILRVKNDESIPFLLVGNKCDLNDKRKVPLSECQLRAQQWAVPYVETSAKTRENVDKVFFDLMREIRSRKTEDSKATSGRAKDRCKKRRLKCTLL

Source Source

Source organism organism	Drosophila melanogaster
Common name common_name	Fruit fly
NCBI taxonomy ID ncbi_taxonomy_id	7227
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	45

▼

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d5cm8b_
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.37.1.0 — automated matches

CATH v4.4 (3 domains)

Domain ID domain_id	5cm8A01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	870 — Son of sevenless (SoS) protein; Chain S, domain 1
Homologous superfamily homologous superfamily	10 — Son of sevenless (SoS) protein Chain: S domain 1

Domain ID domain_id	5cm8A02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	840 — Son of Sevenless (SoS) protein; Chain S, domain 2
Homologous superfamily homologous superfamily	10 — Ras guanine-nucleotide exchange factors catalytic domain

Domain ID domain_id	5cm8B00
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

▶

Unit-cell length a length_a	111.110 Å
Unit-cell length b length_b	98.490 Å
Unit-cell length c length_c	71.320 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	91.61 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

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

Resolution resolution	2.600 Å
Low-resolution limit resolution_low	44.420 Å
R factor r_factor	0.2621
R_work r_work	0.2590
R_free r_free	0.3219

Structural Basis for the Selectivity of Guanine Nucleotide Exchange Factors for the small G-protein Ral

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

Ral guanine nucleotide dissociation stimulator-like 2

State in the Current Structure

Other States of the Same Protein in the Database

Ras-related protein Ral-a

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

5cm8__assembly_1__model_1

5cm8__assembly_1__model_1 | I(q)

5cm8__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (1 domains)

CATH v4.4 (3 domains)

7. Citations (1)

Structural Basis for the Selectivity of Guanine Nucleotide Exchange Factors for the small G-protein Ral

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

Ral guanine nucleotide dissociation stimulator-like 2

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Ras-related protein Ral-a

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

5cm8__assembly_1__model_1

5cm8__assembly_1__model_1 | I(q)

5cm8__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (1 domains)

CATH v4.4 (3 domains)

7. Citations (1)