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2k9a

The Solution Structure of the Arl2 Effector, BART

Method: SOLUTION NMR Dmax: 48.8 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

ADP-ribosylation factor-like protein 2-binding protein

Homo sapiens

UniProt Q9Y2Y0

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 1–136 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions：pH 6；298 K；Ionic strength (raw mmCIF value) 20；Pressure ambient NMR sample composition：1 mM [U-100% 15N] protein, 50 mM sodium phosphate, 150 mM sodium chloride, 0.05 % sodium azide, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition：1 mM [U-100% 13C; U-100% 15N] protein, 50 mM sodium phosphate, 150 mM sodium chloride, 0.05 % sodium azide, 90% H2O/10% D2O | 90% H2O/10% D2O 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 2K9A Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
3DOE Complex of ARL2 and BART, Crystal Form 1 Deposited 2008-07-04 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–163（163 aa）
Not recorded GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；277 K；0.1M bicine, 10% PEG 6000, 20mM hexammine cobalt (III) chloride, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.25 Å R-free 0.261
3DOF Complex of ARL2 and BART, Crystal Form 2 Deposited 2008-07-04 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–163（163 aa）
Not recorded GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.9；293 K；0.2M MgCl2, 20% PEG 3350, pH 5.9, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 3.30 Å R-free 0.294

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AR2BP_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 2–137； UniProt 1–136

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.

SAXS scattering curve SAXS Profile

SAXS profile for 2k9a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2k9a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2k9a
Deposition date deposition_date2008-10-06
Structure title titleThe Solution Structure of the Arl2 Effector, BART
Keywords keywordsProtein, Effector, small G protein, Alternative splicing, Cytoplasm, Mitochondrion, Phosphoprotein, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier18.77 Å
Radius of gyration Rg (electron density) rg_electron18.37 Å
Forward intensity I(0) i08343380000.00
Molecular weight molecular_weight799590.0 kDa
Excluded volume excluded_volume1003300 ų
Envelope volume envelope_volume99053 ų
Hydration-shell volume shell_volume29459 ų
Envelope diameter envelope_diameter90.7 Å
Shell Rg shell_rg34.89 Å
Envelope Rg envelope_rg30.40 Å
Shape Rg shape_rg18.32 Å
Total Rg total_rg18.70 Å
Total atoms total_atoms109450
Residues n_residues6800
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax48.8 Å
Rg (real space) rg_real17.28 Å
Rg uncertainty (real space) rg_real_error0.08 Å
I(0) (real space) i0_real7.8830e+09
I(0) uncertainty (real space) i0_real_error6.4150e+07
Rg (reciprocal space) rg_reciprocal19.00 Å
I(0) (reciprocal space) i0_reciprocal8343000000.0000
Solution quality estimate total_estimate0.6798
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary18.7 Å
Skewness Skewness skewness0.286
Kurtosis Kurtosis kurtosis-0.407
Angular range angular_range— – 0.4250 Å−1
Current regularization parameter α current_alpha3.1850
Highest regularization parameter α highest_alpha454300.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.008; Oscil: 0.959; Stabil: 0.987; Sysdev: 0.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000
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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) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2k9aA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1520 — Adp-ribosylation factor-like protein 2-binding protein fold
Homologous superfamily homologous superfamily10 — ADP-ribosylation factor-like 2-binding protein, domain
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8. Citations (1)

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9. Files and Curves (10)