4k24

Structure of anti-uPAR Fab ATN-658 in complex with uPAR

Method: X-RAY DIFFRACTION Dmax: 143.9 Å Quality: REASONABLE

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

Urokinase-type plasminogen activator

Homo sapiens

UniProt P00749

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 5 其他Polymer 2 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 21–153 Fragment:UNP residues 21-153 Vitronectin × 1 (P04004) anti-uPAR antibody, heavy chain × 1 anti-uPAR antibody, light chain × 1 Urokinase plasminogen activator surface receptor × 1 (Q03405) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 MAN alpha-D-mannopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;295 K;0.1M HEPES pH 7.5, 55%(v/v) Tacsimate, 2%(v/v) 2-methyl-1,3-propanediol, vapor diffusion, sitting drop, temperature 295K Resolution 4.50 Å R-free 0.275

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.

147 other PDB entries and 165 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UROK_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–135; UniProt 21–153

Vitronectin

Homo sapiens

UniProt P04004

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 5 其他Polymer 2 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 21–60 Fragment:UNP residues 21-60 Urokinase-type plasminogen activator × 1 (P00749) anti-uPAR antibody, heavy chain × 1 anti-uPAR antibody, light chain × 1 Urokinase plasminogen activator surface receptor × 1 (Q03405) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 MAN alpha-D-mannopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;295 K;0.1M HEPES pH 7.5, 55%(v/v) Tacsimate, 2%(v/v) 2-methyl-1,3-propanediol, vapor diffusion, sitting drop, temperature 295K Resolution 4.50 Å R-free 0.275

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.

8 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VTNC_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–40; UniProt 21–60

Urokinase plasminogen activator surface receptor

Homo sapiens

UniProt Q03405

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 5 其他Polymer 2 PDB declaration: pentameric(5) Consistent with protein copy count Chain U; UniProt 23–303 Fragment:UNP residues 23-303 Urokinase-type plasminogen activator × 1 (P00749) Vitronectin × 1 (P04004) anti-uPAR antibody, heavy chain × 1 anti-uPAR antibody, light chain × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 MAN alpha-D-mannopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;295 K;0.1M HEPES pH 7.5, 55%(v/v) Tacsimate, 2%(v/v) 2-methyl-1,3-propanediol, vapor diffusion, sitting drop, temperature 295K Resolution 4.50 Å R-free 0.275

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.

11 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UPAR_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain U; PDBConstruct 3–283; UniProt 23–303

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 4k24

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4k24
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id4k24
Deposition date deposition_date2013-04-08
Structure title titleStructure of anti-uPAR Fab ATN-658 in complex with uPAR
Keywords keywordsIMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier41.56
Radius of gyration Rg (electron density) rg_electron42.20
Forward intensity I(0) i0161892000.00
Molecular weight molecular_weight97004.0 kDa
Excluded volume excluded_volume118700 ų
Envelope volume envelope_volume166000 ų
Hydration-shell volume shell_volume36017 ų
Envelope diameter envelope_diameter149.2
Shell Rg shell_rg41.89
Envelope Rg envelope_rg42.27
Shape Rg shape_rg42.17
Total Rg total_rg42.29
Total atoms total_atoms6771
Residues n_residues857
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 dmax143.9
Rg (real space) rg_real42.11
Rg uncertainty (real space) rg_real_error1.80
I(0) (real space) i0_real1.6190e+08
I(0) uncertainty (real space) i0_real_error2.8270e+06
Rg (reciprocal space) rg_reciprocal41.56
I(0) (reciprocal space) i0_reciprocal161800000.0000
Solution quality estimate total_estimate0.7432
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary30.3
Skewness Skewness skewness0.580
Kurtosis Kurtosis kurtosis-0.469
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10680000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.563; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.564; Smooth: 0.405

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)