1l1n

POLIOVIRUS 3C PROTEINASE

Method: X-RAY DIFFRACTION Dmax: 79.3 Å Quality: GOOD

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

Genome polyprotein: Picornain 3C

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 1565–1747 Fragment:Residues 1565-1747 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;293 K;ammonium sulfate, glycerol, mercaptoethanol, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.10 Å R-free 0.259
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1565–1747 Fragment:Residues 1565-1747 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;293 K;ammonium sulfate, glycerol, mercaptoethanol, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.10 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.

80 other PDB entries and 249 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POLH_POL1M
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–183; UniProt 1565–1747 Author chain B; PDBConstruct 1–183; UniProt 1565–1747

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 1l1n

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1l1n
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1l1n
Deposition date deposition_date2002-02-19
Structure title titlePOLIOVIRUS 3C PROTEINASE
Keywords keywordsBETA BARREL, TRYPSIN-LIKE, CATALYTIC TRIAD, Viral protein, hydrolase; Viral protein, hydrolase
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.39
Radius of gyration Rg (electron density) rg_electron22.61
Forward intensity I(0) i025368100.00
Molecular weight molecular_weight38262.0 kDa
Excluded volume excluded_volume47853 ų
Envelope volume envelope_volume56709 ų
Hydration-shell volume shell_volume21689 ų
Envelope diameter envelope_diameter77.9
Shell Rg shell_rg28.83
Envelope Rg envelope_rg22.63
Shape Rg shape_rg22.62
Total Rg total_rg23.35
Total atoms total_atoms2687
Residues n_residues358
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 dmax79.3
Rg (real space) rg_real23.47
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real2.5370e+07
I(0) uncertainty (real space) i0_real_error3.7150e+05
Rg (reciprocal space) rg_reciprocal23.45
I(0) (reciprocal space) i0_reciprocal25370000.0000
Solution quality estimate total_estimate0.8620
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.4
Skewness Skewness skewness0.430
Kurtosis Kurtosis kurtosis-0.410
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9636000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.764; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.927; Smooth: 0.983

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1l1na_
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_idd1l1nb_
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

CATH v4.4 (4 domains)

Domain ID domain_id1l1nA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1l1nA02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1l1nB01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1l1nB02
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)