1cqq

TYPE 2 RHINOVIRUS 3C PROTEASE WITH AG7088 INHIBITOR

Method: X-RAY DIFFRACTION Dmax: 53.6 Å Quality: GOOD

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

TYPE 2 RHINOVIRUS 3C PROTEASE

OrganismNot specified

UniProt P04936

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 1508–1687 Not recorded AG7 4-{2-(4-FLUORO-BENZYL)-6-METHYL-5-[(5-METHYL-ISOXAZOLE-3-CARBONYL)-AMINO]-4-OXO-HEPTANOYLAMINO}-5-(2-OXO-PYRROLIDIN-3-YL)-PENTANOIC ACID ETHYL ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;286 K;20% PEG10K, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 13K Resolution 1.85 Å

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.

17 other PDB entries and 48 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POLG_HRV2
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–180; UniProt 1508–1687

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 1cqq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1cqq
Deposition date deposition_date1999-08-10
Structure title titleTYPE 2 RHINOVIRUS 3C PROTEASE WITH AG7088 INHIBITOR
Keywords keywordsVIRAL PROTEIN, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.48
Radius of gyration Rg (electron density) rg_electron15.03
Forward intensity I(0) i07638510.00
Molecular weight molecular_weight20338.0 kDa
Excluded volume excluded_volume25510 ų
Envelope volume envelope_volume27817 ų
Hydration-shell volume shell_volume15220 ų
Envelope diameter envelope_diameter51.9
Shell Rg shell_rg21.44
Envelope Rg envelope_rg15.36
Shape Rg shape_rg15.02
Total Rg total_rg16.20
Total atoms total_atoms1783
Residues n_residues180
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 dmax53.6
Rg (real space) rg_real16.33
Rg uncertainty (real space) rg_real_error0.29
I(0) (real space) i0_real7.6390e+06
I(0) uncertainty (real space) i0_real_error9.1630e+04
Rg (reciprocal space) rg_reciprocal16.35
I(0) (reciprocal space) i0_reciprocal7639000.0000
Solution quality estimate total_estimate0.8727
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.7
Skewness Skewness skewness0.054
Kurtosis Kurtosis kurtosis-0.428
Angular range angular_range— – 0.4850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2488000.0000
Real-space data points n_real_points79
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.788; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1cqqa_
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 (2 domains)

Domain ID domain_id1cqqA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1cqqA02
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)