5z7l

Crystal structure of NDP52 SKICH region in complex with NAP1

Method: X-RAY DIFFRACTION Dmax: 77.7 Å Quality: EXCELLENT

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

Calcium-binding and coiled-coil domain-containing protein 2

Homo sapiens

UniProt Q13137

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 10–126 Chain B; UniProt 10–126 Fragment:UNP residues 10-126 5-azacytidine-induced protein 2 × 2 (Q9H6S1) GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;PEG3350,sodium malonate Resolution 2.02 Å R-free 0.222

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.

9 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CACO2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–117; UniProt 10–126 Author chain B; PDBConstruct 1–117; UniProt 10–126

5-azacytidine-induced protein 2

Homo sapiens

UniProt Q9H6S1

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 33–75 Chain D; UniProt 33–75 Fragment:UNP residues 33-75 Calcium-binding and coiled-coil domain-containing protein 2 × 2 (Q13137) GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;PEG3350,sodium malonate Resolution 2.02 Å R-free 0.222

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.

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

View Construct and Data Evidence
UniProt name AZI2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–43; UniProt 33–75 Author chain D; PDBConstruct 1–43; UniProt 33–75

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 5z7l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5z7l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5z7l
Deposition date deposition_date2018-01-29
Structure title titleCrystal structure of NDP52 SKICH region in complex with NAP1
Keywords keywordsNDP52, NAP1, SKICH, Autophagy, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.31
Radius of gyration Rg (electron density) rg_electron23.67
Forward intensity I(0) i021539900.00
Molecular weight molecular_weight36718.0 kDa
Excluded volume excluded_volume46521 ų
Envelope volume envelope_volume57349 ų
Hydration-shell volume shell_volume21219 ų
Envelope diameter envelope_diameter80.6
Shell Rg shell_rg29.33
Envelope Rg envelope_rg24.26
Shape Rg shape_rg23.62
Total Rg total_rg24.60
Total atoms total_atoms2601
Residues n_residues305
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 dmax77.7
Rg (real space) rg_real24.34
Rg uncertainty (real space) rg_real_error0.57
I(0) (real space) i0_real2.1540e+07
I(0) uncertainty (real space) i0_real_error3.0990e+05
Rg (reciprocal space) rg_reciprocal24.33
I(0) (reciprocal space) i0_reciprocal21540000.0000
Solution quality estimate total_estimate0.9016
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.4
Skewness Skewness skewness0.293
Kurtosis Kurtosis kurtosis-0.575
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6495000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.938; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.923; Smooth: 0.981

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id5z7lA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily2840
Domain ID domain_id5z7lB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily2840

8. Citations (1)

9. Files and Curves (10)