3mce

Crystal structure of the NAC domain of alpha subunit of nascent polypeptide-associated complex(NAC)

Method: X-RAY DIFFRACTION Dmax: 75.6 Å Quality: GOOD

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

Nascent polypeptide-associated complex subunit alpha

Homo sapiens

UniProt Q13765

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 81–133 Chain B; UniProt 81–133 Fragment:NAC domain (UNP RESIDUES 81-133) IOD IODIDE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.3;289 K;0.2M potassium citrate tribasic monohydrate (pH 8.3), 20% (w/v) PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.40 Å R-free 0.277
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 81–133 Chain D; UniProt 81–133 Fragment:NAC domain (UNP RESIDUES 81-133) IOD IODIDE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.3;289 K;0.2M potassium citrate tribasic monohydrate (pH 8.3), 20% (w/v) PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.40 Å R-free 0.277

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.

24 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NACA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 9–61; UniProt 81–133 Author chain B; PDBConstruct 9–61; UniProt 81–133 Author chain C; PDBConstruct 9–61; UniProt 81–133 Author chain D; PDBConstruct 9–61; UniProt 81–133

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 3mce

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3mce
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3mce
Deposition date deposition_date2010-03-29
Structure title titleCrystal structure of the NAC domain of alpha subunit of nascent polypeptide-associated complex(NAC)
Keywords keywordsbeta-barrel like structure, NAC, homodimer, Chaperone; CHAPERONE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.45
Radius of gyration Rg (electron density) rg_electron20.15
Forward intensity I(0) i012900900.00
Molecular weight molecular_weight26830.0 kDa
Excluded volume excluded_volume33428 ų
Envelope volume envelope_volume39523 ų
Hydration-shell volume shell_volume17508 ų
Envelope diameter envelope_diameter76.5
Shell Rg shell_rg25.68
Envelope Rg envelope_rg20.56
Shape Rg shape_rg19.94
Total Rg total_rg21.58
Total atoms total_atoms1831
Residues n_residues233
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 dmax75.6
Rg (real space) rg_real21.58
Rg uncertainty (real space) rg_real_error0.61
I(0) (real space) i0_real1.2900e+07
I(0) uncertainty (real space) i0_real_error1.7880e+05
Rg (reciprocal space) rg_reciprocal21.56
I(0) (reciprocal space) i0_reciprocal12900000.0000
Solution quality estimate total_estimate0.8321
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.2
Skewness Skewness skewness0.506
Kurtosis Kurtosis kurtosis-0.202
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1491000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.677; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.838; Smooth: 0.945

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)