4x1r

The crystal structure of mupain-1-12 in complex with murinised human uPA at pH7.4

Method: X-RAY DIFFRACTION Dmax: 58.9 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 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain U; UniProt 179–425 Fragment:catalytic domain (UNP RESIDUES 179-425) Mutation:H99Y, C122A, N145Q mupain-1-12 × 1 PL0 1-phenylguanidine × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;298 K;2.0M ammonium sulfate, 50mM sodium citrate pH 4.6, 5% PEG 400 Resolution 2.10 Å R-free 0.273

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 2
Chains and sequence ranges Author chain U; PDBConstruct 1–247; UniProt 179–425

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 4x1r

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4x1r
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4x1r
Deposition date deposition_date2014-11-25
Structure title titleThe crystal structure of mupain-1-12 in complex with murinised human uPA at pH7.4
Keywords keywordsSerine protease, peptidic inhibitor, uPA, HYDROLASE INHIBITOR-HYDROLASE complex; HYDROLASE INHIBITOR/HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.26
Radius of gyration Rg (electron density) rg_electron17.05
Forward intensity I(0) i015262800.00
Molecular weight molecular_weight29043.0 kDa
Excluded volume excluded_volume36144 ų
Envelope volume envelope_volume39771 ų
Hydration-shell volume shell_volume18932 ų
Envelope diameter envelope_diameter59.9
Shell Rg shell_rg23.90
Envelope Rg envelope_rg17.43
Shape Rg shape_rg17.03
Total Rg total_rg18.09
Total atoms total_atoms2038
Residues n_residues238
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 dmax58.9
Rg (real space) rg_real18.15
Rg uncertainty (real space) rg_real_error0.28
I(0) (real space) i0_real1.5260e+07
I(0) uncertainty (real space) i0_real_error1.6460e+05
Rg (reciprocal space) rg_reciprocal18.16
I(0) (reciprocal space) i0_reciprocal15260000.0000
Solution quality estimate total_estimate0.7234
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.9
Skewness Skewness skewness0.163
Kurtosis Kurtosis kurtosis-0.327
Angular range angular_range— – 0.4350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5677000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.825; Stabil: 1.000; Sysdev: 0.330; Positv: 1.000; Valcen: 0.988; Smooth: 0.950

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id4x1rU01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id4x1rU02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases

8. Citations (1)

9. Files and Curves (10)