2mmg

Structural Characterization of the Mengovirus Leader Protein Bound to Ran GTPase by Nuclear Magnetic Resonance

Method: SOLUTION NMR Dmax: 63.7 Å Quality: GOOD

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

GTP-binding nuclear protein Ran

Homo sapiens

UniProt P62826

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 1–216 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7.4;298 K;Ionic strength (raw mmCIF value) 102;Pressure ambient NMR sample composition:0.5 mM [U-100% 13C; U-100% 15N] Ran GTPase, 0.5 mM L Mengo, 20 mM HEPES, 100 mM potassium chloride, 2 mM magnesium chloride, 2 mM DTT, 0.04 % sodium azide, 90% H2O/10% D2O | 90% H2O/10% D2O Resolution not provided

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.

137 other PDB entries and 203 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAN_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–216; UniProt 1–216

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 2mmg

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2mmg
Deposition date deposition_date2014-03-15
Structure title titleStructural Characterization of the Mengovirus Leader Protein Bound to Ran GTPase by Nuclear Magnetic Resonance
Keywords keywords;G-protein, nucleotide binding, GTP binding, virus-host interactions, GTPase, nuclear pore complex, leader, cardioviruses, nucleocytoplasmic transport, nucleus, TRANSPORT PROTEIN ;; TRANSPORT PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier18.34
Radius of gyration Rg (electron density) rg_electron17.89
Forward intensity I(0) i0786768000.00
Molecular weight molecular_weight244230.0 kDa
Excluded volume excluded_volume308710 ų
Envelope volume envelope_volume62673 ų
Hydration-shell volume shell_volume24309 ų
Envelope diameter envelope_diameter71.4
Shell Rg shell_rg28.77
Envelope Rg envelope_rg22.27
Shape Rg shape_rg17.85
Total Rg total_rg18.35
Total atoms total_atoms34490
Residues n_residues2160
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 dmax63.7
Rg (real space) rg_real18.29
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real7.8680e+08
I(0) uncertainty (real space) i0_real_error1.0680e+07
Rg (reciprocal space) rg_reciprocal18.30
I(0) (reciprocal space) i0_reciprocal786800000.0000
Solution quality estimate total_estimate0.7775
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary23.3
Skewness Skewness skewness0.336
Kurtosis Kurtosis kurtosis-0.022
Angular range angular_range— – 0.4350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1779000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.702; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2mmga_
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.37.1.8 — G proteins

CATH v4.4 (1 domains)

Domain ID domain_id2mmgA00
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)