2cpg

TRANSCRIPTIONAL REPRESSOR COPG

Method: X-RAY DIFFRACTION Dmax: 54.8 Å Quality: GOOD

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

TRANSCRIPTIONAL REPRESSOR COPG

Streptococcus agalactiae

UniProt P13920

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–45 Chain B; UniProt 1–45 Fragment:DNA-BINDING PROTEIN CL CHLORIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.7;72% MPD, 0.1 M HEPES PH 6.7, 3% BENZAMIDINE Resolution 1.60 Å R-free 0.277
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–45 Fragment:DNA-BINDING PROTEIN CL CHLORIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.7;72% MPD, 0.1 M HEPES PH 6.7, 3% BENZAMIDINE Resolution 1.60 Å R-free 0.277

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.

2 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COPG_STRAG
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–45; UniProt 1–45 Author chain B; PDBConstruct 1–45; UniProt 1–45 Author chain C; PDBConstruct 1–45; UniProt 1–45

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 2cpg

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2cpg
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2cpg
Deposition date deposition_date1999-11-15
Structure title titleTRANSCRIPTIONAL REPRESSOR COPG
Keywords keywordsTRANSCRIPTIONAL REPRESSOR, DNA-BINDING PROTEIN, PLASMID, GENE REGULATION; GENE REGULATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.49
Radius of gyration Rg (electron density) rg_electron15.31
Forward intensity I(0) i04461130.00
Molecular weight molecular_weight14795.0 kDa
Excluded volume excluded_volume18634 ų
Envelope volume envelope_volume23107 ų
Hydration-shell volume shell_volume13021 ų
Envelope diameter envelope_diameter53.5
Shell Rg shell_rg20.80
Envelope Rg envelope_rg15.75
Shape Rg shape_rg15.30
Total Rg total_rg16.52
Total atoms total_atoms1019
Residues n_residues130
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 dmax54.8
Rg (real space) rg_real16.42
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real4.4610e+06
I(0) uncertainty (real space) i0_real_error5.2990e+04
Rg (reciprocal space) rg_reciprocal16.43
I(0) (reciprocal space) i0_reciprocal4461000.0000
Solution quality estimate total_estimate0.8673
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.4
Skewness Skewness skewness0.269
Kurtosis Kurtosis kurtosis-0.149
Angular range angular_range— – 0.4850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha801600.0000
Real-space data points n_real_points79
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.769; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.965

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2cpga_
Class classa — All alpha proteins
Fold Fold folda.43 — Ribbon-helix-helix
Superfamily Superfamily superfamilya.43.1 — Ribbon-helix-helix
Family Family familya.43.1.3 — CopG-like
Domain ID domain_idd2cpgb_
Class classa — All alpha proteins
Fold Fold folda.43 — Ribbon-helix-helix
Superfamily Superfamily superfamilya.43.1 — Ribbon-helix-helix
Family Family familya.43.1.3 — CopG-like
Domain ID domain_idd2cpgc_
Class classa — All alpha proteins
Fold Fold folda.43 — Ribbon-helix-helix
Superfamily Superfamily superfamilya.43.1 — Ribbon-helix-helix
Family Family familya.43.1.3 — CopG-like

CATH v4.4 (3 domains)

Domain ID domain_id2cpgA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1220 — Arc Repressor Mutant
Homologous superfamily homologous superfamily10 — Met repressor-like
Domain ID domain_id2cpgB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1220 — Arc Repressor Mutant
Homologous superfamily homologous superfamily10 — Met repressor-like
Domain ID domain_id2cpgC00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1220 — Arc Repressor Mutant
Homologous superfamily homologous superfamily10 — Met repressor-like

8. Citations (2)

9. Files and Curves (10)