6mfn

Human Argonaute2-miR-27a bound to HSUR1 target RNA

Method: X-RAY DIFFRACTION Dmax: 100.6 Å Quality: GOOD

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

Protein argonaute-2

Homo sapiens

UniProt Q9UKV8

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–RNA Monomer Protein × 1 RNA 2 PDB declaration: trimeric(3) Consistent with all polymer counts Chain A; UniProt 1–859 Mutation:D669A, S387D, S824A, S828D, S831D, S834A ;RNA (5'-R(P*UP*UP*CP*AP*CP*AP*GP*UP*G)-3') ; × 1 ;RNA (5'-R(P*UP*CP*UP*GP*UP*GP*AP*UP*AP*A)-3') ; × 1 IPH PHENOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;10% PEG3350, 50 mM Tris, pH 8.0, 20 mM magnesium chloride, 75 mM phenol Resolution 2.50 Å R-free 0.247

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.

66 other PDB entries and 96 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AGO2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–859; UniProt 1–859

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 6mfn

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6mfn
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6mfn
Deposition date deposition_date2018-09-11
Structure title titleHuman Argonaute2-miR-27a bound to HSUR1 target RNA
Keywords keywordsRNA-binding protein, microRNA, target directed microRNA decay, HYDROLASE-RNA complex; HYDROLASE/RNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.46
Radius of gyration Rg (electron density) rg_electron31.22
Forward intensity I(0) i0160334000.00
Molecular weight molecular_weight97411.0 kDa
Excluded volume excluded_volume120580 ų
Envelope volume envelope_volume157400 ų
Hydration-shell volume shell_volume41828 ų
Envelope diameter envelope_diameter109.9
Shell Rg shell_rg38.45
Envelope Rg envelope_rg31.17
Shape Rg shape_rg31.22
Total Rg total_rg31.81
Total atoms total_atoms6823
Residues n_residues822
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 dmax100.6
Rg (real space) rg_real31.42
Rg uncertainty (real space) rg_real_error0.77
I(0) (real space) i0_real1.6030e+08
I(0) uncertainty (real space) i0_real_error2.3990e+06
Rg (reciprocal space) rg_reciprocal31.44
I(0) (reciprocal space) i0_reciprocal160300000.0000
Solution quality estimate total_estimate0.8262
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.2
Skewness Skewness skewness0.295
Kurtosis Kurtosis kurtosis-0.433
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha35390000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.912; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id6mfnA02
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology260 — paz domain
Homologous superfamily homologous superfamily10 — paz domain
Domain ID domain_id6mfnA03
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator
Domain ID domain_id6mfnA04
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily10 — Ribonuclease H-like superfamily/Ribonuclease H

8. Citations (1)

9. Files and Curves (10)