3n4m

E. coli RNA polymerase alpha subunit C-terminal domain in complex with CAP and DNA

Method: X-RAY DIFFRACTION Dmax: 90.8 Å Quality: REASONABLE

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

Catabolite gene activator

Escherichia coli

UniProt P0ACJ8

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–DNA Heteromer Protein × 6 DNA 4 PDB declaration: decameric(10) Consistent with all polymer counts Chain A; UniProt 2–210 Not recorded DNA-directed RNA polymerase subunit alpha × 4 (P0A7Z4) ;DNA (5'-D(*CP*TP*TP*TP*TP*TP*TP*CP*CP*TP*AP*AP*AP*AP*TP*GP*TP*GP*AP*T)-3') ; × 2 ;DNA (5'-D(*CP*TP*AP*GP*AP*TP*CP*AP*CP*AP*TP*TP*TP*TP*AP*GP*GP*AP*AP*AP*AP*AP*AP*G)-3') ; × 2 CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 4 PEG DI(HYDROXYETHYL)ETHER × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;293.2 K;100 mM sodium acetate (pH 4.5), 625 mM NaCl, VAPOR DIFFUSION, HANGING DROP, temperature 293.2K Resolution 2.99 Å R-free 0.224

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.

39 other PDB entries and 43 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CRP_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–209; UniProt 2–210

DNA-directed RNA polymerase subunit alpha

Escherichia coli

UniProt P0A7Z4

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–DNA Heteromer Protein × 6 DNA 4 PDB declaration: decameric(10) Consistent with all polymer counts Chain B; UniProt 246–329 Chain C; UniProt 246–329 Fragment:alpha subunit C-terminal domain, residues 246-329 Catabolite gene activator × 2 (P0ACJ8) ;DNA (5'-D(*CP*TP*TP*TP*TP*TP*TP*CP*CP*TP*AP*AP*AP*AP*TP*GP*TP*GP*AP*T)-3') ; × 2 ;DNA (5'-D(*CP*TP*AP*GP*AP*TP*CP*AP*CP*AP*TP*TP*TP*TP*AP*GP*GP*AP*AP*AP*AP*AP*AP*G)-3') ; × 2 CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE × 4 PEG DI(HYDROXYETHYL)ETHER × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;293.2 K;100 mM sodium acetate (pH 4.5), 625 mM NaCl, VAPOR DIFFUSION, HANGING DROP, temperature 293.2K Resolution 2.99 Å R-free 0.224

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.

276 other PDB entries and 305 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOA_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–84; UniProt 246–329 Author chain C; PDBConstruct 1–84; UniProt 246–329

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 3n4m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3n4m
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3n4m
Deposition date deposition_date2010-05-21
Structure title titleE. coli RNA polymerase alpha subunit C-terminal domain in complex with CAP and DNA
Keywords keywordsprotein-protein interactions, protein-DNA interactions, GENE REGULATION-DNA complex; GENE REGULATION/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.62
Radius of gyration Rg (electron density) rg_electron26.05
Forward intensity I(0) i062681400.00
Molecular weight molecular_weight53496.0 kDa
Excluded volume excluded_volume63544 ų
Envelope volume envelope_volume85685 ų
Hydration-shell volume shell_volume28191 ų
Envelope diameter envelope_diameter94.4
Shell Rg shell_rg32.34
Envelope Rg envelope_rg25.76
Shape Rg shape_rg26.09
Total Rg total_rg26.57
Total atoms total_atoms3702
Residues n_residues394
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 dmax90.8
Rg (real space) rg_real26.51
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real6.2680e+07
I(0) uncertainty (real space) i0_real_error7.8870e+05
Rg (reciprocal space) rg_reciprocal26.55
I(0) (reciprocal space) i0_reciprocal62680000.0000
Solution quality estimate total_estimate0.6861
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary34.8
Skewness Skewness skewness0.178
Kurtosis Kurtosis kurtosis-0.384
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4691000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.831; Stabil: 1.000; Sysdev: 0.145; Positv: 1.000; Valcen: 0.990; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd3n4ma1
Class classb — All beta proteins
Fold Fold foldb.82 — Double-stranded beta-helix
Superfamily Superfamily superfamilyb.82.3 — cAMP-binding domain-like
Family Family familyb.82.3.2 — cAMP-binding domain
Domain ID domain_idd3n4ma2
Class classa — All alpha proteins
Fold Fold folda.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamilya.4.5 — 'Winged helix' DNA-binding domain
Family Family familya.4.5.4 — CAP C-terminal domain-like
Domain ID domain_idd3n4mb_
Class classa — All alpha proteins
Fold Fold folda.60 — SAM domain-like
Superfamily Superfamily superfamilya.60.3 — C-terminal domain of RNA polymerase alpha subunit
Family Family familya.60.3.1 — C-terminal domain of RNA polymerase alpha subunit
Domain ID domain_idd3n4mc_
Class classa — All alpha proteins
Fold Fold folda.60 — SAM domain-like
Superfamily Superfamily superfamilya.60.3 — C-terminal domain of RNA polymerase alpha subunit
Family Family familya.60.3.1 — C-terminal domain of RNA polymerase alpha subunit

CATH v4.4 (4 domains)

Domain ID domain_id3n4mA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily10 — Jelly Rolls
Domain ID domain_id3n4mA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily10 — Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain
Domain ID domain_id3n4mB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily20 — 5' to 3' exonuclease, C-terminal subdomain
Domain ID domain_id3n4mC00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily20 — 5' to 3' exonuclease, C-terminal subdomain

8. Citations (2)

9. Files and Curves (10)