5zkp

Crystal structure of the human platelet-activating factor receptor in complex with SR 27417

Method: X-RAY DIFFRACTION Dmax: 105.6 Å Quality: REASONABLE

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

Platelet-activating factor receptor,Flavodoxin,Platelet-activating factor receptor

Homo sapiens

UniProt P00323

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 2–148 Mutation:F116Y, N169D,P2A, Y98W,A230D, V234A, D289N 9ER N1,N1-dimethyl-N2-[(pyridin-3-yl)methyl]-N2-{4-[2,4,6-tri(propan-2-yl)phenyl]-1,3-thiazol-2-yl}ethane-1,2-diamine × 1 FMN FLAVIN MONONUCLEOTIDE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC CUBIC PHASE;293 K;HEPES, PEG 400, NaSCN, Na citrate Resolution 2.81 Å R-free 0.259

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.

39 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLAV_DESVH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 219–365; UniProt 2–148

Platelet-activating factor receptor,Flavodoxin,Platelet-activating factor receptor

Homo sapiens

UniProt P25105

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 2–216 Chain A; UniProt 224–316 Mutation:F116Y, N169D,P2A, Y98W,A230D, V234A, D289N 9ER N1,N1-dimethyl-N2-[(pyridin-3-yl)methyl]-N2-{4-[2,4,6-tri(propan-2-yl)phenyl]-1,3-thiazol-2-yl}ethane-1,2-diamine × 1 FMN FLAVIN MONONUCLEOTIDE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC CUBIC PHASE;293 K;HEPES, PEG 400, NaSCN, Na citrate Resolution 2.81 Å R-free 0.259

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.

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

View Construct and Data Evidence
UniProt name PTAFR_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–218; UniProt 2–216 Author chain A; PDBConstruct 366–458; UniProt 224–316

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 5zkp

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5zkp
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5zkp
Deposition date deposition_date2018-03-25
Structure title titleCrystal structure of the human platelet-activating factor receptor in complex with SR 27417
Keywords keywordsG protein-coupled receptor, Platelet-activating factor receptor, Complex, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.64
Radius of gyration Rg (electron density) rg_electron29.80
Forward intensity I(0) i035460100.00
Molecular weight molecular_weight48888.0 kDa
Excluded volume excluded_volume62145 ų
Envelope volume envelope_volume78579 ų
Hydration-shell volume shell_volume24653 ų
Envelope diameter envelope_diameter111.5
Shell Rg shell_rg33.17
Envelope Rg envelope_rg29.66
Shape Rg shape_rg29.84
Total Rg total_rg30.02
Total atoms total_atoms3450
Residues n_residues436
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 dmax105.6
Rg (real space) rg_real31.06
Rg uncertainty (real space) rg_real_error1.00
I(0) (real space) i0_real3.5460e+07
I(0) uncertainty (real space) i0_real_error5.6190e+05
Rg (reciprocal space) rg_reciprocal30.88
I(0) (reciprocal space) i0_reciprocal35460000.0000
Solution quality estimate total_estimate0.5739
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.4
Skewness Skewness skewness0.545
Kurtosis Kurtosis kurtosis-0.499
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9954000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.584; Stabil: 1.000; Sysdev: 0.193; Positv: 1.000; Valcen: 0.386; Smooth: 0.740

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)