SAXSdb — 2sxl

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

SEX-LETHAL PROTEIN

Drosophila melanogaster

UniProt P19339

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 122–209	Fragment：RNA-BINDING DOMAIN 1 (RBD1), RESIDUES 122 - 209 Mutation：F166Y	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 4；298 K	Resolution not provided

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 2SXL	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1B7F SXL-LETHAL PROTEIN/RNA COMPLEX Deposited 1999-01-23	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Monomer；Protein × 1 PDB declaration: dimeric	Chain A 82–249（168 aa） Fragment：2 RNP-DOMAINS	Mutation：F166Y	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；pH 7.0, VAPOR DIFFUSION, HANGING DROP	Resolution 2.60 Å R-free 0.294
1B7F SXL-LETHAL PROTEIN/RNA COMPLEX Deposited 1999-01-23	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein–RNA Monomer；Protein × 1 PDB declaration: dimeric	Chain B 82–249（168 aa） Fragment：2 RNP-DOMAINS	Mutation：F166Y	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；pH 7.0, VAPOR DIFFUSION, HANGING DROP	Resolution 2.60 Å R-free 0.294
1SXL RESONANCE ASSIGNMENTS AND SOLUTION STRUCTURE OF THE SECOND RNA-BINDING DOMAIN OF SEX-LETHAL DETERMINED BY MULTIDIMENSIONAL HETERONUCLEAR MAGNETIC RESONANCE SPECTROSCOPY Deposited 1994-07-01	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 199–294（96 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
3SXL SEX-LETHAL RNA RECOGNITION DOMAINS 1 AND 2 FROM DROSOPHILA MELANOGASTER Deposited 1999-04-04	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 111–294（184 aa） Fragment：RNA BINDING DOMAINS 1 AND 2 (RESIDUES 112-294 OF FULL LENGTH)	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.8；pH 7.80	Resolution 2.70 Å R-free 0.264
3SXL SEX-LETHAL RNA RECOGNITION DOMAINS 1 AND 2 FROM DROSOPHILA MELANOGASTER Deposited 1999-04-04	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 111–294（184 aa） Fragment：RNA BINDING DOMAINS 1 AND 2 (RESIDUES 112-294 OF FULL LENGTH)	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.8；pH 7.80	Resolution 2.70 Å R-free 0.264
3SXL SEX-LETHAL RNA RECOGNITION DOMAINS 1 AND 2 FROM DROSOPHILA MELANOGASTER Deposited 1999-04-04	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 111–294（184 aa） Fragment：RNA BINDING DOMAINS 1 AND 2 (RESIDUES 112-294 OF FULL LENGTH)	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.8；pH 7.80	Resolution 2.70 Å R-free 0.264
4QQB Structural basis for the assembly of the SXL-UNR translation regulatory complex Deposited 2014-06-27	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 2 PDB declaration: trimeric	Chain A 122–294（173 aa） Fragment：RRM1-RRM2, UNP residues 122-294	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；277 K；0.1 M LiSO4, PEG3350 1-5 %, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.80 Å R-free 0.236
4QQB Structural basis for the assembly of the SXL-UNR translation regulatory complex Deposited 2014-06-27	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein–RNA Heteromer；Protein × 2 PDB declaration: trimeric	Chain B 122–294（173 aa） Fragment：RRM1-RRM2, UNP residues 122-294	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；277 K；0.1 M LiSO4, PEG3350 1-5 %, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.80 Å R-free 0.236

4 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	SXL_DROME
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–88； UniProt 122–209

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	2sxl
Deposition date deposition_date	1997-07-16
Structure title title	SEX-LETHAL RBD1, NMR, MINIMIZED AVERAGE STRUCTURE
Keywords keywords	RNA-BINDING DOMAIN, ALTERNATIVE SPLICING, RIKEN Structural Genomics/Proteomics Initiative, RSGI, Structural Genomics; RNA-BINDING DOMAIN
Experimental Method method	SOLUTION NMR

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	14.37 Å
Radius of gyration Rg (electron density) rg_electron	12.93 Å
Forward intensity I(0) i0	2205320.00
Molecular weight molecular_weight	10054.0 kDa
Excluded volume excluded_volume	12586 Å³
Envelope volume envelope_volume	14551 Å³
Hydration-shell volume shell_volume	9839 Å³
Envelope diameter envelope_diameter	46.2 Å
Shell Rg shell_rg	18.30 Å
Envelope Rg envelope_rg	13.56 Å
Shape Rg shape_rg	12.88 Å
Total Rg total_rg	14.35 Å
Total atoms total_atoms	1418
Residues n_residues	88
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	48.7 Å
Rg (real space) rg_real	14.31 Å
Rg uncertainty (real space) rg_real_error	0.35 Å
I(0) (real space) i0_real	2.2050e+06
I(0) uncertainty (real space) i0_real_error	2.6070e+04
Rg (reciprocal space) rg_reciprocal	14.31 Å
I(0) (reciprocal space) i0_reciprocal	2205000.0000
Solution quality estimate total_estimate	0.8739
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	17.9 Å
Skewness Skewness skewness	0.176
Kurtosis Kurtosis kurtosis	-0.297
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	327900.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.790; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.989

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d2sxla_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.58 — Ferredoxin-like
Superfamily Superfamily superfamily	d.58.7 — RNA-binding domain, RBD, aka RNA recognition motif (RRM)
Family Family family	d.58.7.1 — Canonical RBD

CATH v4.4 (1 domains)

Domain ID domain_id	2sxlA00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	330 — RRM (RNA recognition motif) domain

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8. Citations (6)

;A characteristic arrangement of aromatic amino acid residues in the solution structure of the amino-terminal RNA-binding domain of Drosophila sex-lethal. ;

J.Mol.Biol. (1997)

PMID: 9299339 · DOI: 10.1006/jmbi.1997.1213 PRIMARY

Crystal Structure at 1.92 A Resolution of the RNA-Binding Domain of the U1A Spliceosomal Protein Complexed with an RNA Hairpin

Nature (1994)

;Resonance Assignments and Solution Structure of the Second RNA-Binding Domain of Sex-Lethal Determined by Multidimensional Heteronuclear Magnetic Resonance ;

Biochemistry (1994)

;Determination of the Secondary Structure and Folding Topology of an RNA Binding Domain of Mammalian Hnrnp A1 Protein Using Three-Dimensional Heteronuclear Magnetic Resonance Spectroscopy ;

Biochemistry (1994)

1H, 13C, and 15N NMR Assignments and Global Folding Pattern of the RNA-Binding Domain of the Human Hnrnp C Proteins

Biochemistry (1992)

Crystal Structure of the RNA-Binding Domain of the U1 Small Nuclear Ribonucleoprotein A

Nature (1990)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Description description	SEX-LETHAL PROTEIN
Molecular weight formula_weight	10061.5 kDa
Mutation mutation	F166Y
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1418

来源生物 organism	Drosophila melanogaster
通用名 common_name	fruit fly
NCBI Class编号 ncbi_taxonomy_id	7227
宿主生物 host_organism	Escherichia coli BL21(DE3)

SEX-LETHAL RBD1, NMR, MINIMIZED AVERAGE STRUCTURE

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

SEX-LETHAL PROTEIN

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (6)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/sx/2sxl/2sxl.fit
pddf	/app/data/pr_computation/sx/2sxl/2sxl.pr.out
profile	/app/data/saxs_computation/sx/2sxl/2sxl.dat