7ea2

crystal structure of NAP1 FIR in complex with RB1CC1 Claw domain

Method: X-RAY DIFFRACTION Dmax: 70.0 Å Quality: GOOD

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

5-azacytidine-induced protein 2,RB1-inducible coiled-coil protein 1

Homo sapiens

UniProt Q8TDY2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1490–1594 Chain B; UniProt 1490–1594 Not recorded P6G HEXAETHYLENE GLYCOL × 1 PEG DI(HYDROXYETHYL)ETHER × 2 FLC CITRATE ANION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;0.1 M phosphate/citrate pH 4.2, 40% PEG300 Resolution 2.14 Å R-free 0.232

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.

17 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBCC1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 20–124; UniProt 1490–1594 Author chain B; PDBConstruct 20–124; UniProt 1490–1594

5-azacytidine-induced protein 2,RB1-inducible coiled-coil protein 1

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 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 6–16 Chain B; UniProt 6–16 Not recorded P6G HEXAETHYLENE GLYCOL × 1 PEG DI(HYDROXYETHYL)ETHER × 2 FLC CITRATE ANION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;0.1 M phosphate/citrate pH 4.2, 40% PEG300 Resolution 2.14 Å R-free 0.232

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 1
Chains and sequence ranges Author chain A; PDBConstruct 5–15; UniProt 6–16 Author chain B; PDBConstruct 5–15; UniProt 6–16

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 7ea2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7ea2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7ea2
Deposition date deposition_date2021-03-06
Structure title titlecrystal structure of NAP1 FIR in complex with RB1CC1 Claw domain
Keywords keywordsFIR, complex, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.02
Radius of gyration Rg (electron density) rg_electron19.82
Forward intensity I(0) i011189500.00
Molecular weight molecular_weight25850.0 kDa
Excluded volume excluded_volume32791 ų
Envelope volume envelope_volume39398 ų
Hydration-shell volume shell_volume17477 ų
Envelope diameter envelope_diameter72.8
Shell Rg shell_rg25.35
Envelope Rg envelope_rg19.90
Shape Rg shape_rg19.77
Total Rg total_rg20.85
Total atoms total_atoms1823
Residues n_residues218
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 dmax70.0
Rg (real space) rg_real21.06
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real1.1190e+07
I(0) uncertainty (real space) i0_real_error1.5320e+05
Rg (reciprocal space) rg_reciprocal21.05
I(0) (reciprocal space) i0_reciprocal11190000.0000
Solution quality estimate total_estimate0.8029
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary22.3
Skewness Skewness skewness0.377
Kurtosis Kurtosis kurtosis-0.405
Angular range angular_range— – 0.3800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3019000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.834; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.935; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)