1s77

T7 RNAP product pyrophosphate elongation complex

Method: X-RAY DIFFRACTION Dmax: 100.1 Å Quality: GOOD

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

DNA-directed RNA polymerase

Enterobacteria phage T7

UniProt P00573

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Monomer Protein × 1 DNA 2 RNA 1 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain D; UniProt 1–883 Not recorded ;DNA (5'-D(*GP*CP*CP*GP*TP*GP*CP*GP*CP*AP*TP*TP*CP*GP*CP*CP*GP*TP*GP*TP*T)-3') ; × 1 ;DNA (5'-D(*TP*TP*TP*AP*CP*GP*TP*TP*GP*CP*GP*CP*AP*CP*GP*GP*C)-3') ; × 1 ;RNA (5'-R(*AP*CP*AP*CP*GP*GP*CP*GP*AP*(3DA))-3') ; × 1 MG MAGNESIUM ION × 2 POP PYROPHOSPHATE 2- × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.2;298 K;T7RNAP, DNA,RNA, 3'deoxyATP, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.69 Å R-free 0.285

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.

18 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOL_BPT7
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–883; UniProt 1–883

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 1s77

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1s77
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1s77
Deposition date deposition_date2004-01-29
Structure title titleT7 RNAP product pyrophosphate elongation complex
Keywords keywordsT7 RNA polymerase, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.47
Radius of gyration Rg (electron density) rg_electron30.14
Forward intensity I(0) i0216012000.00
Molecular weight molecular_weight107980.0 kDa
Excluded volume excluded_volume131230 ų
Envelope volume envelope_volume169830 ų
Hydration-shell volume shell_volume45830 ų
Envelope diameter envelope_diameter106.3
Shell Rg shell_rg38.17
Envelope Rg envelope_rg30.00
Shape Rg shape_rg30.16
Total Rg total_rg30.74
Total atoms total_atoms7539
Residues n_residues875
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 dmax100.1
Rg (real space) rg_real30.34
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real2.1600e+08
I(0) uncertainty (real space) i0_real_error2.7920e+06
Rg (reciprocal space) rg_reciprocal30.40
I(0) (reciprocal space) i0_reciprocal216000000.0000
Solution quality estimate total_estimate0.8814
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.5
Skewness Skewness skewness0.251
Kurtosis Kurtosis kurtosis-0.316
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha48600000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.832; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.959

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1s77d_
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.8.1.3 — T7 RNA polymerase

CATH v4.4 (5 domains)

Domain ID domain_id1s77D01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1320 — T7 RNA polymerase; domain 1
Homologous superfamily homologous superfamily10 — DNA-directed RNA polymerase, N-terminal domain
Domain ID domain_id1s77D02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily260
Domain ID domain_id1s77D03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily370
Domain ID domain_id1s77D04
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily280
Domain ID domain_id1s77D05
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 (1)

9. Files and Curves (10)