4dcd

1.6A resolution structure of PolioVirus 3C Protease Containing a covalently bound dipeptidyl inhibitor

Method: X-RAY DIFFRACTION Dmax: 56.1 Å Quality: REASONABLE

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

Genome polyprotein

Human poliovirus 1

UniProt P03300

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 1566–1748 Fragment:unp residues 1566-1748 DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 1 K36 (1S,2S)-2-({N-[(benzyloxy)carbonyl]-L-leucyl}amino)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propane-1-sulfonic acid × 1 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;298 K;30% (w/v) PEG 5000 MME, 100 mM MES, 200 mM ammonium sulfate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 1.69 Å R-free 0.189

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.

80 other PDB entries and 250 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POLG_POL1M
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 8–190; UniProt 1566–1748

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 4dcd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4dcd
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id4dcd
Deposition date deposition_date2012-01-17
Structure title title1.6A resolution structure of PolioVirus 3C Protease Containing a covalently bound dipeptidyl inhibitor
Keywords keywordsPROTEASE, POLIOVIRUS, ANTIVIRAL INHIBITORS, DIPEPTIDYL INHIBITOR, HYDROLASE-HYDROLASE INHIBITOR complex; HYDROLASE/HYDROLASE INHIBITOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.98
Radius of gyration Rg (electron density) rg_electron15.39
Forward intensity I(0) i08017580.00
Molecular weight molecular_weight20151.0 kDa
Excluded volume excluded_volume24993 ų
Envelope volume envelope_volume27762 ų
Hydration-shell volume shell_volume15069 ų
Envelope diameter envelope_diameter55.5
Shell Rg shell_rg21.61
Envelope Rg envelope_rg15.78
Shape Rg shape_rg15.38
Total Rg total_rg16.48
Total atoms total_atoms1413
Residues n_residues184
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 dmax56.1
Rg (real space) rg_real16.87
Rg uncertainty (real space) rg_real_error0.27
I(0) (real space) i0_real8.0180e+06
I(0) uncertainty (real space) i0_real_error9.2290e+04
Rg (reciprocal space) rg_reciprocal16.88
I(0) (reciprocal space) i0_reciprocal8018000.0000
Solution quality estimate total_estimate0.7465
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.9
Skewness Skewness skewness0.152
Kurtosis Kurtosis kurtosis-0.320
Angular range angular_range— – 0.4700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1912000.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.780; Stabil: 1.000; Sysdev: 0.456; Positv: 1.000; Valcen: 0.999; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4dcda1
Class classb — All beta proteins
Fold Fold foldb.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamilyb.47.1 — Trypsin-like serine proteases
Family Family familyb.47.1.4 — Viral cysteine protease of trypsin fold
Domain ID domain_idd4dcda2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id4dcdA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id4dcdA02
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)