6b1q

Hydrogen Bonding Complementary, not size complementarity is key in the formation of the double helix

Method: X-RAY DIFFRACTION Dmax: 71.5 Å Quality: EXCELLENT

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

Reverse transcriptase

Moloney murine leukemia virus

UniProt P03355

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 4 PDB declaration: hexameric(6) Consistent with all polymer counts Chain A; UniProt 683–937 Fragment:Catalytic fragment (UNP residues 683-937) ;DNA (5'-D(*CP*TP*TP*AP*TP*(CJ1)P*(CJ1)P*(CJ1))-3') ; × 2 ;DNA (5'-D(P*(1AP)P*(1AP)P*(1AP)P*AP*TP*AP*AP*G)-3') ; × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277.15 K;6 % PEG 4000, 5 mM magnesium acetate and 50 mM ADA (pH 6.5) Resolution 1.90 Å R-free 0.237

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.

44 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POL_MLVMS
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–259; UniProt 683–937

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 6b1q

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6b1q
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6b1q
Deposition date deposition_date2017-09-18
Structure title titleHydrogen Bonding Complementary, not size complementarity is key in the formation of the double helix
Keywords keywordsProtein-DNA, AEGIS, unnatural base pair, host-guest system, DNA BINDING PROTEIN, DNA BINDING PROTEIN-DNA complex; DNA BINDING PROTEIN/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.07
Radius of gyration Rg (electron density) rg_electron21.66
Forward intensity I(0) i020722400.00
Molecular weight molecular_weight32534.0 kDa
Excluded volume excluded_volume39741 ų
Envelope volume envelope_volume49794 ų
Hydration-shell volume shell_volume19639 ų
Envelope diameter envelope_diameter74.1
Shell Rg shell_rg27.75
Envelope Rg envelope_rg21.55
Shape Rg shape_rg21.60
Total Rg total_rg22.55
Total atoms total_atoms2279
Residues n_residues252
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 dmax71.5
Rg (real space) rg_real23.02
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real2.0720e+07
I(0) uncertainty (real space) i0_real_error2.6180e+05
Rg (reciprocal space) rg_reciprocal23.03
I(0) (reciprocal space) i0_reciprocal20720000.0000
Solution quality estimate total_estimate0.9160
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.5
Skewness Skewness skewness0.179
Kurtosis Kurtosis kurtosis-0.635
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2184000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.972; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id6b1qA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily270 — Reverse transcriptase/Diguanylate cyclase domain
Domain ID domain_id6b1qA02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology10 — HIV Type 1 Reverse Transcriptase; Chain A, domain 1
Homologous superfamily homologous superfamily10 — HIV Type 1 Reverse Transcriptase, subunit A, domain 1

8. Citations (1)

9. Files and Curves (10)