1i6v

THERMUS AQUATICUS CORE RNA POLYMERASE-RIFAMPICIN COMPLEX

Method: X-RAY DIFFRACTION Dmax: 140.0 Å Quality: REASONABLE

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

DNA-DIRECTED RNA POLYMERASE

OrganismNot specified

UniProt Q9KWU8

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–314 Chain B; UniProt 1–314 Fragment:ALPHA SUBUNIT DNA-DIRECTED RNA POLYMERASE × 1 (Q9KWU7) DNA-DIRECTED RNA POLYMERASE × 1 (Q9KWU6) DNA-DIRECTED RNA POLYMERASE × 1 (Q9EVV4) RFP RIFAMPICIN × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;298 K;Tris-HCl, Ammonium Sulfate, Magensium Chloride, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.30 Å R-free 0.359

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.

12 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOA_THEAQ
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–314; UniProt 1–314 Author chain B; PDBConstruct 1–314; UniProt 1–314

DNA-DIRECTED RNA POLYMERASE

OrganismNot specified

UniProt Q9KWU7

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 1–1119 Fragment:BETA SUBUNIT DNA-DIRECTED RNA POLYMERASE × 2 (Q9KWU8) DNA-DIRECTED RNA POLYMERASE × 1 (Q9KWU6) DNA-DIRECTED RNA POLYMERASE × 1 (Q9EVV4) RFP RIFAMPICIN × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;298 K;Tris-HCl, Ammonium Sulfate, Magensium Chloride, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.30 Å R-free 0.359

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.

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

View Construct and Data Evidence
UniProt name RPOB_THEAQ
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–1118; UniProt 1–1119

DNA-DIRECTED RNA POLYMERASE

OrganismNot specified

UniProt Q9KWU6

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 1–1524 Fragment:BETA-PRIME SUBUNIT DNA-DIRECTED RNA POLYMERASE × 2 (Q9KWU8) DNA-DIRECTED RNA POLYMERASE × 1 (Q9KWU7) DNA-DIRECTED RNA POLYMERASE × 1 (Q9EVV4) RFP RIFAMPICIN × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;298 K;Tris-HCl, Ammonium Sulfate, Magensium Chloride, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.30 Å R-free 0.359

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.

13 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOC_THEAQ
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–1264; UniProt 1–1524

DNA-DIRECTED RNA POLYMERASE

OrganismNot specified

UniProt Q9EVV4

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 1–99 Fragment:OMEGA SUBUNIT DNA-DIRECTED RNA POLYMERASE × 2 (Q9KWU8) DNA-DIRECTED RNA POLYMERASE × 1 (Q9KWU7) DNA-DIRECTED RNA POLYMERASE × 1 (Q9KWU6) RFP RIFAMPICIN × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;298 K;Tris-HCl, Ammonium Sulfate, Magensium Chloride, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.30 Å R-free 0.359

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.

11 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPOZ_THEAQ
Isoform
PDB entities 4
Chains and sequence ranges Author chain E; PDBConstruct 1–99; UniProt 1–99

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 1i6v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1i6v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1i6v
Deposition date deposition_date2001-03-05
Structure title titleTHERMUS AQUATICUS CORE RNA POLYMERASE-RIFAMPICIN COMPLEX
Keywords keywordsTRANSFERASE, TRANSCRIPTION, DNA-DIRECTED RNA POLYMERASE, 3D- STRUCTURE; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier46.30
Radius of gyration Rg (electron density) rg_electron45.83
Forward intensity I(0) i01335720000.00
Molecular weight molecular_weight301940.0 kDa
Excluded volume excluded_volume377920 ų
Envelope volume envelope_volume547610 ų
Hydration-shell volume shell_volume95483 ų
Envelope diameter envelope_diameter233.2
Shell Rg shell_rg52.90
Envelope Rg envelope_rg47.90
Shape Rg shape_rg45.88
Total Rg total_rg45.94
Total atoms total_atoms21292
Residues n_residues2839
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 dmax140.0
Rg (real space) rg_real45.21
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real1.2860e+09
I(0) uncertainty (real space) i0_real_error1.9580e+07
Rg (reciprocal space) rg_reciprocal46.30
I(0) (reciprocal space) i0_reciprocal1335000000.0000
Solution quality estimate total_estimate0.7142
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary57.6
Skewness Skewness skewness0.270
Kurtosis Kurtosis kurtosis-0.172
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha1.9580
Highest regularization parameter α highest_alpha211800000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.003; Oscil: 0.898; Stabil: 0.933; Sysdev: 0.000; Positv: 1.000; Valcen: 0.960; Smooth: 0.846

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 21 domains

SCOP 2.08 (7 domains)

Domain ID domain_idd1i6va1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.74 — DCoH-like
Superfamily Superfamily superfamilyd.74.3 — RBP11-like subunits of RNA polymerase
Family Family familyd.74.3.1 — RNA polymerase alpha subunit dimerisation domain
Domain ID domain_idd1i6va2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.181 — Insert subdomain of RNA polymerase alpha subunit
Superfamily Superfamily superfamilyd.181.1 — Insert subdomain of RNA polymerase alpha subunit
Family Family familyd.181.1.1 — Insert subdomain of RNA polymerase alpha subunit
Domain ID domain_idd1i6vb1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.74 — DCoH-like
Superfamily Superfamily superfamilyd.74.3 — RBP11-like subunits of RNA polymerase
Family Family familyd.74.3.1 — RNA polymerase alpha subunit dimerisation domain
Domain ID domain_idd1i6vb2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.181 — Insert subdomain of RNA polymerase alpha subunit
Superfamily Superfamily superfamilyd.181.1 — Insert subdomain of RNA polymerase alpha subunit
Family Family familyd.181.1.1 — Insert subdomain of RNA polymerase alpha subunit
Domain ID domain_idd1i6vc_
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.29 — beta and beta-prime subunits of DNA dependent RNA-polymerase
Superfamily Superfamily superfamilye.29.1 — beta and beta-prime subunits of DNA dependent RNA-polymerase
Family Family familye.29.1.1 — RNA-polymerase beta
Domain ID domain_idd1i6vd_
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.29 — beta and beta-prime subunits of DNA dependent RNA-polymerase
Superfamily Superfamily superfamilye.29.1 — beta and beta-prime subunits of DNA dependent RNA-polymerase
Family Family familye.29.1.2 — RNA-polymerase beta-prime
Domain ID domain_idd1i6ve_
Class classa — All alpha proteins
Fold Fold folda.143 — RPB6/omega subunit-like
Superfamily Superfamily superfamilya.143.1 — RPB6/omega subunit-like
Family Family familya.143.1.1 — RNA polymerase omega subunit

CATH v4.4 (14 domains)

Domain ID domain_id1i6vA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1360 — Gyrase A; domain 2
Homologous superfamily homologous superfamily10 — RNA polymerase, RBP11-like subunit
Domain ID domain_id1i6vA02
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology120 — RNA Polymerase Alpha Subunit; Chain A, domain 2
Homologous superfamily homologous superfamily12 — DNA-directed RNA polymerase, insert domain
Domain ID domain_id1i6vB01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1360 — Gyrase A; domain 2
Homologous superfamily homologous superfamily10 — RNA polymerase, RBP11-like subunit
Domain ID domain_id1i6vB02
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology120 — RNA Polymerase Alpha Subunit; Chain A, domain 2
Homologous superfamily homologous superfamily12 — DNA-directed RNA polymerase, insert domain
Domain ID domain_id1i6vC01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology270 — Dna-directed Rna Polymerase Ii 140kd Polypeptide; Chain: B; Domain 6
Homologous superfamily homologous superfamily10 — DNA-directed RNA polymerase, subunit 2, domain 6
Domain ID domain_id1i6vC02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1100 — Rna Polymerase Beta Subunit; Chain: C,domain 2
Homologous superfamily homologous superfamily10
Domain ID domain_id1i6vC03
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1110 — Dna-directed Rna Polymerase Ii 140kd Polypeptide; Chain: B; domain 3
Homologous superfamily homologous superfamily10 — RNA polymerase Rpb2, domain 2
Domain ID domain_id1i6vC04
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology150 — Rna Polymerase Beta Subunit; Chain: C, domain 4
Homologous superfamily homologous superfamily10 — DNA-directed RNA polymerase, beta subunit, external 1 domain
Domain ID domain_id1i6vC05
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily100 — RNA polymerase II/Efflux pump adaptor protein, barrel-sandwich hybrid domain
Domain ID domain_id1i6vC06
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily150 — RNA polymerase II, Rpb2 subunit, wall domain
Domain ID domain_id1i6vD02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology274 — Enzyme I; Chain A, domain 2
Homologous superfamily homologous superfamily100 — RNA polymerase Rpb1, domain 3
Domain ID domain_id1i6vD03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology132 — Topoisomerase I; Chain A, domain 4
Homologous superfamily homologous superfamily30 — RNA polymerase Rpb1 funnel domain
Domain ID domain_id1i6vD05
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology105 — Molybdopterin biosynthesis moea protein, domain 2
Homologous superfamily homologous superfamily10 — Molybdopterin biosynthesis moea protein, domain 2
Domain ID domain_id1i6vE00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology940 — Eukaryotic RPB6 RNA polymerase subunit
Homologous superfamily homologous superfamily10 — RNA polymerase subunit, RPB6/omega

8. Citations (1)

9. Files and Curves (10)