2gk7

Structural and Functional insights into the human Upf1 helicase core

Method: X-RAY DIFFRACTION Dmax: 80.0 Å Quality: EXCELLENT

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

Regulator of nonsense transcripts 1

Homo sapiens

UniProt Q92900

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 295–914 Fragment:helicase core domain(residues 295-914) PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 5.8;295 K;100mM Na/K Phosphate, 6-8% PEG3350, 10mM DTT, pH 5.8, EVAPORATION, temperature 295K Resolution 2.80 Å R-free 0.298

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.

11 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RENT1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–624; UniProt 295–914

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 2gk7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2gk7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2gk7
Deposition date deposition_date2006-03-31
Structure title titleStructural and Functional insights into the human Upf1 helicase core
Keywords keywordsUpf1, helicase, NMD, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.21
Radius of gyration Rg (electron density) rg_electron25.23
Forward intensity I(0) i073419100.00
Molecular weight molecular_weight67190.0 kDa
Excluded volume excluded_volume84424 ų
Envelope volume envelope_volume104510 ų
Hydration-shell volume shell_volume33516 ų
Envelope diameter envelope_diameter82.0
Shell Rg shell_rg33.40
Envelope Rg envelope_rg25.31
Shape Rg shape_rg25.25
Total Rg total_rg26.06
Total atoms total_atoms4724
Residues n_residues596
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 dmax80.0
Rg (real space) rg_real26.06
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real7.3420e+07
I(0) uncertainty (real space) i0_real_error1.0010e+06
Rg (reciprocal space) rg_reciprocal26.11
I(0) (reciprocal space) i0_reciprocal73420000.0000
Solution quality estimate total_estimate0.9089
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.8
Skewness Skewness skewness0.138
Kurtosis Kurtosis kurtosis-0.537
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16630000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.944; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.990

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2gk7a1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.19 — Tandem AAA-ATPase domain
Domain ID domain_idd2gk7a2
Class classb — All beta proteins
Fold Fold foldb.49 — Domain of alpha and beta subunits of F1 ATP synthase-like
Superfamily Superfamily superfamilyb.49.4 — Upf1 barrel domain-like
Family Family familyb.49.4.1 — Upf1 barrel domain-like
Domain ID domain_idd2gk7a3
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.19 — Tandem AAA-ATPase domain

CATH v4.4 (4 domains)

Domain ID domain_id2gk7A01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id2gk7A02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily230
Domain ID domain_id2gk7A03
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology140 — Helix Hairpins
Homologous superfamily homologous superfamily1240
Domain ID domain_id2gk7A04
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases

8. Citations (1)

9. Files and Curves (10)