1qpz

PURINE REPRESSOR-HYPOXANTHINE-PALINDROMIC OPERATOR COMPLEX

Method: X-RAY DIFFRACTION Dmax: 100.9 Å Quality: REASONABLE

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

PROTEIN (PURINE NUCLEOTIDE SYNTHESIS REPRESSOR)

Escherichia coli

UniProt P0ACP7

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 Homooligomer Protein × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain A; UniProt 1–340 Not recorded ;DNA (5'-D(*TP*AP*CP*GP*CP*AP*AP*AP*CP*GP*TP*TP*TP*GP*CP*GP*T)-3') ; × 2 HPA HYPOXANTHINE × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.50 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.

25 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PURR_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–340; UniProt 1–340

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 1qpz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1qpz
Deposition date deposition_date1999-06-01
Structure title titlePURINE REPRESSOR-HYPOXANTHINE-PALINDROMIC OPERATOR COMPLEX
Keywords keywordsTRANSCRIPTION REGULATION, DNA-BINDING, REPRESSOR, PURINE BIOSYNTHESIS, COMPLEX (DNA-BINDING PROTEIN-DNA), TRANSCRIPTION-DNA COMPLEX; TRANSCRIPTION/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.10
Radius of gyration Rg (electron density) rg_electron29.04
Forward intensity I(0) i036743000.00
Molecular weight molecular_weight43203.0 kDa
Excluded volume excluded_volume52407 ų
Envelope volume envelope_volume70008 ų
Hydration-shell volume shell_volume22826 ų
Envelope diameter envelope_diameter106.6
Shell Rg shell_rg32.41
Envelope Rg envelope_rg29.47
Shape Rg shape_rg28.99
Total Rg total_rg29.52
Total atoms total_atoms3012
Residues n_residues356
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 dmax100.9
Rg (real space) rg_real30.46
Rg uncertainty (real space) rg_real_error0.91
I(0) (real space) i0_real3.6740e+07
I(0) uncertainty (real space) i0_real_error5.5070e+05
Rg (reciprocal space) rg_reciprocal30.31
I(0) (reciprocal space) i0_reciprocal36740000.0000
Solution quality estimate total_estimate0.6163
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.7
Skewness Skewness skewness0.529
Kurtosis Kurtosis kurtosis-0.502
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5138000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.711; Stabil: 1.000; Sysdev: 0.135; Positv: 1.000; Valcen: 0.560; Smooth: 0.910

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1qpza1
Class classa — All alpha proteins
Fold Fold folda.35 — lambda repressor-like DNA-binding domains
Superfamily Superfamily superfamilya.35.1 — lambda repressor-like DNA-binding domains
Family Family familya.35.1.5 — GalR/LacI-like bacterial regulator
Domain ID domain_idd1qpza2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.93 — Periplasmic binding protein-like I
Superfamily Superfamily superfamilyc.93.1 — Periplasmic binding protein-like I
Family Family familyc.93.1.1 — L-arabinose binding protein-like

CATH v4.4 (3 domains)

Domain ID domain_id1qpzA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology260 — 434 Repressor (Amino-terminal Domain)
Homologous superfamily homologous superfamily40 — lambda repressor-like DNA-binding domains
Domain ID domain_id1qpzA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator
Domain ID domain_id1qpzA03
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator

8. Citations (2)

9. Files and Curves (10)