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2xc7

Solution Structure of PHAX-RBD in complex with ssRNA

Method: SOLUTION NMR Dmax: 63.3 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

PHOSPHORYLATED ADAPTER RNA EXPORT PROTEIN

HOMO SAPIENS

UniProt Q9H814

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 1 PDB declaration: dimeric（2） Consistent with all polymer counts Chain A； UniProt 223–323 Fragment：RNA_GG_BIND, RESIDUES 223-323 5'-(AP*UP*CP*GP)-3' × 1 SOLUTION NMR NMR measurement conditions：pH 6.5；297 K；Ionic strength (raw mmCIF value) 50 NMR sample composition：90% WATER/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.

Other PDB Difference from Current Entry 2XC7 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
8PNT Structure of the human nuclear cap-binding complex bound to PHAX and m7G-capped RNA Deposited 2023-07-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 1–394（394 aa）
Chain D 1–394（394 aa）
Not recorded MGT 7N-METHYL-8-HYDROGUANOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.46 Å
9HFL Cryo-EM structure of the human snRNA export complex comprising CBC-PHAX-CRM1-RanGTP and capped-RNA Deposited 2024-11-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–RNA Heteromer；Protein × 6 PDB declaration: heptameric
Chain N 1–394（394 aa）
Chain P 1–394（394 aa）
Not recorded GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 GTA P1-7-METHYLGUANOSINE-P3-ADENOSINE-5',5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.62 Å

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PHAX_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 4–104； UniProt 223–323

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 2xc7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2xc7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2xc7
Deposition date deposition_date2010-04-18
Structure title titleSolution Structure of PHAX-RBD in complex with ssRNA
Keywords keywordsRNA BINDING PROTEIN, PROTEIN-RNA COMPLEX, NUCLEAR EXPORT; RNA BINDING PROTEIN
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier15.64 Å
Radius of gyration Rg (electron density) rg_electron15.00 Å
Forward intensity I(0) i0279445000.00
Molecular weight molecular_weight130360.0 kDa
Excluded volume excluded_volume159740 ų
Envelope volume envelope_volume40908 ų
Hydration-shell volume shell_volume18099 ų
Envelope diameter envelope_diameter69.4 Å
Shell Rg shell_rg25.79 Å
Envelope Rg envelope_rg20.58 Å
Shape Rg shape_rg14.97 Å
Total Rg total_rg15.51 Å
Total atoms total_atoms17220
Residues n_residues1080
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax63.3 Å
Rg (real space) rg_real15.73 Å
Rg uncertainty (real space) rg_real_error0.60 Å
I(0) (real space) i0_real2.7940e+08
I(0) uncertainty (real space) i0_real_error3.5780e+06
Rg (reciprocal space) rg_reciprocal15.72 Å
I(0) (reciprocal space) i0_reciprocal279400000.0000
Solution quality estimate total_estimate0.7401
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.4 Å
Skewness Skewness skewness0.602
Kurtosis Kurtosis kurtosis0.433
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha620100.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.358; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.554; Smooth: 0.992
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2xc7A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily1440 — PHAX RNA-binding domain
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8. Citations (1)

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9. Files and Curves (10)