4z4g

Human Argonaute2 Bound to t1-Inosine Target RNA

Method: X-RAY DIFFRACTION Dmax: 95.1 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:S387D ;RNA (5'-R(P*UP*UP*CP*AP*CP*AP*UP*UP*GP*CP*CP*CP*AP*AP*GP*UP*CP*UP*UP*U)-3') ; × 1 ;RNA (5'-R(*CP*AP*AP*UP*GP*UP*GP*A)-D(P*(IMP))-3') ; × 1 MG MAGNESIUM ION × 3 IPH PHENOL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;PEG 3350, Tris, Isopropanol, Phenol, Magnesium Resolution 2.70 Å R-free 0.224

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 4z4g

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4z4g
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4z4g
Deposition date deposition_date2015-04-02
Structure title titleHuman Argonaute2 Bound to t1-Inosine Target RNA
Keywords keywordsArgonaute2, gene regulation-rna complex; gene regulation/rna
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.19
Radius of gyration Rg (electron density) rg_electron30.11
Forward intensity I(0) i0175924000.00
Molecular weight molecular_weight100240.0 kDa
Excluded volume excluded_volume123250 ų
Envelope volume envelope_volume156390 ų
Hydration-shell volume shell_volume42622 ų
Envelope diameter envelope_diameter102.4
Shell Rg shell_rg37.88
Envelope Rg envelope_rg30.26
Shape Rg shape_rg30.11
Total Rg total_rg30.75
Total atoms total_atoms7007
Residues n_residues827
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 dmax95.1
Rg (real space) rg_real30.14
Rg uncertainty (real space) rg_real_error0.61
I(0) (real space) i0_real1.7590e+08
I(0) uncertainty (real space) i0_real_error2.4300e+06
Rg (reciprocal space) rg_reciprocal30.16
I(0) (reciprocal space) i0_reciprocal175900000.0000
Solution quality estimate total_estimate0.8942
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.7
Skewness Skewness skewness0.315
Kurtosis Kurtosis kurtosis-0.383
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha38390000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.920; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.860

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id4z4gA02
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology260 — paz domain
Homologous superfamily homologous superfamily10 — paz domain
Domain ID domain_id4z4gA03
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator
Domain ID domain_id4z4gA04
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)