4mpa

Crystal structure of NHERF1-CXCR2 signaling complex in P21 space group

Method: X-RAY DIFFRACTION Dmax: 52.6 Å Quality: REASONABLE

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

Na(+)/H(+) exchange regulatory cofactor NHE-RF1, C-X-C chemokine receptor type 2 chimera

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 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 11–94 Fragment:SEE REMARK 999 ACY ACETIC ACID × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.8;293 K;100 mM sodium acetate, pH 4.8, 0.2 M ammonium acetate, 24% PEG4000, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.10 Å R-free 0.157

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 NHRF1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–86; UniProt 11–94

Na(+)/H(+) exchange regulatory cofactor NHE-RF1, C-X-C chemokine receptor type 2 chimera

Homo sapiens

UniProt P25025

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 356–360 Fragment:SEE REMARK 999 ACY ACETIC ACID × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.8;293 K;100 mM sodium acetate, pH 4.8, 0.2 M ammonium acetate, 24% PEG4000, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.10 Å R-free 0.157

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.

20 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CXCR2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 87–91; UniProt 356–360

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 4mpa

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4mpa
Deposition date deposition_date2013-09-12
Structure title titleCrystal structure of NHERF1-CXCR2 signaling complex in P21 space group
Keywords keywordsneutrophil, inflammatory diseases, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier14.33
Radius of gyration Rg (electron density) rg_electron13.20
Forward intensity I(0) i02204250.00
Molecular weight molecular_weight9942.0 kDa
Excluded volume excluded_volume12401 ų
Envelope volume envelope_volume14827 ų
Hydration-shell volume shell_volume9999 ų
Envelope diameter envelope_diameter53.8
Shell Rg shell_rg18.42
Envelope Rg envelope_rg13.90
Shape Rg shape_rg13.16
Total Rg total_rg14.54
Total atoms total_atoms1404
Residues n_residues91
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 dmax52.6
Rg (real space) rg_real14.31
Rg uncertainty (real space) rg_real_error0.52
I(0) (real space) i0_real2.2040e+06
I(0) uncertainty (real space) i0_real_error3.2110e+04
Rg (reciprocal space) rg_reciprocal14.31
I(0) (reciprocal space) i0_reciprocal2204000.0000
Solution quality estimate total_estimate0.7296
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary18.6
Skewness Skewness skewness0.403
Kurtosis Kurtosis kurtosis0.269
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha402800.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.510; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.953; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4mpaa1
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_idd4mpaa2
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_id4mpaA00
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)