2jxo

Structure of the second PDZ domain of NHERF-1

Method: SOLUTION NMR Dmax: 44.4 Å Quality: GOOD

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

Ezrin-radixin-moesin-binding phosphoprotein 50

Homo sapiens

UniProt O14745

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 150–240 Fragment:PDZ 2 domain No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7.5;288.1 K;Ionic strength (raw mmCIF value) 0.15;Pressure ambient NMR sample composition:1 mM PDZ2, HEPES, DTT, H2O, DSS, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:1 mM [U-100% 15N] PDZ2, HEPES, DTT, H2O, DSS, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:1 mM [U-100% 13C; U-100% 15N] PDZ2, HEPES, DTT, H2O, DSS, 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.

21 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NHERF_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 8–98; UniProt 150–240

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 2jxo

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2jxo
Deposition date deposition_date2007-11-27
Structure title titleStructure of the second PDZ domain of NHERF-1
Keywords keywords;NHERF-1, PDZ domain, PDZ2, Acetylation, Cell projection, Membrane, Phosphoprotein, Polymorphism, Wnt signaling pathway, PROTEIN BINDING ;; PROTEIN BINDING
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier13.43
Radius of gyration Rg (electron density) rg_electron13.36
Forward intensity I(0) i0255958000.00
Molecular weight molecular_weight128500.0 kDa
Excluded volume excluded_volume158660 ų
Envelope volume envelope_volume24421 ų
Hydration-shell volume shell_volume13670 ų
Envelope diameter envelope_diameter50.5
Shell Rg shell_rg21.00
Envelope Rg envelope_rg15.66
Shape Rg shape_rg13.36
Total Rg total_rg13.62
Total atoms total_atoms17928
Residues n_residues1176
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 dmax44.4
Rg (real space) rg_real13.37
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real2.5600e+08
I(0) uncertainty (real space) i0_real_error3.0290e+06
Rg (reciprocal space) rg_reciprocal13.37
I(0) (reciprocal space) i0_reciprocal256000000.0000
Solution quality estimate total_estimate0.7973
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary17.4
Skewness Skewness skewness0.182
Kurtosis Kurtosis kurtosis-0.270
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha163300.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.790; Stabil: 0.997; 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 (1)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2jxoa1
Class classb — All beta proteins
Fold Fold foldb.36 — PDZ domain-like
Superfamily Superfamily superfamilyb.36.1 — PDZ domain-like
Family Family familyb.36.1.1 — PDZ domain
Domain ID domain_idd2jxoa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id2jxoA00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology42 — Pdz3 Domain
Homologous superfamily homologous superfamily10 — PDZ domain

8. Citations (1)

9. Files and Curves (10)