1d1u

USE OF AN N-TERMINAL FRAGMENT FROM MOLONEY MURINE LEUKEMIA VIRUS REVERSE TRANSCRIPTASE TO FACILITATE CRYSTALLIZATION AND ANALYSIS OF A PSEUDO-16-MER DNA MOLECULE CONTAINING G-A MISPAIRS

Method: X-RAY DIFFRACTION Dmax: 73.5 Å Quality: EXCELLENT

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

PROTEIN (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 Monomer Protein × 1 DNA 2 PDB declaration: trimeric(3) Consistent with all polymer counts Chain A; UniProt 144–398 Fragment:FINGERS AND PALM DOMAIN OF MMLV RT ;DNA (5'-D(*CP*TP*CP*GP*TP*G)-3') ; × 1 ;DNA (5'-D(*AP*CP*GP*GP*CP*AP*CP*GP*AP*G)-3') ; × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;pH 6.50 Resolution 2.30 Å R-free 0.286

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_MLVMO
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 1–255; UniProt 144–398

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 1d1u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1d1u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1d1u
Deposition date deposition_date1999-09-21
Structure title titleUSE OF AN N-TERMINAL FRAGMENT FROM MOLONEY MURINE LEUKEMIA VIRUS REVERSE TRANSCRIPTASE TO FACILITATE CRYSTALLIZATION AND ANALYSIS OF A PSEUDO-16-MER DNA MOLECULE CONTAINING G-A MISPAIRS
Keywords keywords;G-A MISPAIR, SYN-ADENINE, NUCLEIC ACID, PROTEIN-DNA COMPLEX, SINGLE-STRAND OVERHANG, REVERSE TRANSCRIPTASE, MOLONEY MURINE LEUKEMIA VIRUS, HYDROLASE-DNA COMPLEX ;; HYDROLASE/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.14
Radius of gyration Rg (electron density) rg_electron21.76
Forward intensity I(0) i022356400.00
Molecular weight molecular_weight33762.0 kDa
Excluded volume excluded_volume41248 ų
Envelope volume envelope_volume52005 ų
Hydration-shell volume shell_volume20418 ų
Envelope diameter envelope_diameter74.4
Shell Rg shell_rg27.86
Envelope Rg envelope_rg21.82
Shape Rg shape_rg21.71
Total Rg total_rg22.66
Total atoms total_atoms2365
Residues n_residues271
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 dmax73.5
Rg (real space) rg_real23.09
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real2.2360e+07
I(0) uncertainty (real space) i0_real_error2.7650e+05
Rg (reciprocal space) rg_reciprocal23.10
I(0) (reciprocal space) i0_reciprocal22360000.0000
Solution quality estimate total_estimate0.9110
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.0
Skewness Skewness skewness0.212
Kurtosis Kurtosis kurtosis-0.539
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2213000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.952; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1d1ua_
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.8 — DNA/RNA polymerases
Superfamily Superfamily superfamilye.8.1 — DNA/RNA polymerases
Family Family familye.8.1.2 — Reverse transcriptase

CATH v4.4 (2 domains)

Domain ID domain_id1d1uA01
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
Domain ID domain_id1d1uA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily270 — Reverse transcriptase/Diguanylate cyclase domain

8. Citations (2)

9. Files and Curves (10)