2x6m

Structure of a single domain camelid antibody fragment in complex with a C-terminal peptide of alpha-synuclein

Method: X-RAY DIFFRACTION Dmax: 39.0 Å Quality: REASONABLE

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

ALPHA-SYNUCLEIN PEPTIDE

OrganismNot specified

UniProt P37840

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 132–140 Fragment:C-TERMINAL FRAGMENT OF ALPHA-SYNUCLEIN, RESIDUES 132-140 HEAVY CHAIN VARIABLE DOMAIN FROM DROMEDARY × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;25% PEG6000, 100 MM HEPES PH 7.5, 100 MM LICL Resolution 1.62 Å R-free 0.203

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.

226 other PDB entries and 234 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SYUA_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–9; UniProt 132–140

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 2x6m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2x6m
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2x6m
Deposition date deposition_date2010-02-18
Structure title titleStructure of a single domain camelid antibody fragment in complex with a C-terminal peptide of alpha-synuclein
Keywords keywords;IMMUNE SYSTEM, PARKINSON'S DISEASE, ALZHEIMER DISEASE AMYLOID, NANOBODY, AFFINITY TAG ;; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.16
Radius of gyration Rg (electron density) rg_electron14.02
Forward intensity I(0) i04447370.00
Molecular weight molecular_weight14130.0 kDa
Excluded volume excluded_volume17256 ų
Envelope volume envelope_volume19113 ų
Hydration-shell volume shell_volume11771 ų
Envelope diameter envelope_diameter59.2
Shell Rg shell_rg19.76
Envelope Rg envelope_rg14.63
Shape Rg shape_rg14.04
Total Rg total_rg15.09
Total atoms total_atoms993
Residues n_residues132
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

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

Maximum dimension Dmax dmax39.0
Rg (real space) rg_real14.46
Rg uncertainty (real space) rg_real_error0.04
I(0) (real space) i0_real4.2450e+06
I(0) uncertainty (real space) i0_real_error3.4840e+04
Rg (reciprocal space) rg_reciprocal15.14
I(0) (reciprocal space) i0_reciprocal4447000.0000
Solution quality estimate total_estimate0.6859
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.132
Kurtosis Kurtosis kurtosis-0.498
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha3.5230
Highest regularization parameter α highest_alpha926300.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.002; Oscil: 0.999; Stabil: 0.976; Sysdev: 0.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2x6ma_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)

CATH v4.4 (1 domains)

Domain ID domain_id2x6mA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)