1pcz

STRUCTURE OF TATA-BINDING PROTEIN

Method: X-RAY DIFFRACTION Dmax: 88.3 Å Quality: GOOD

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

TATA-BINDING PROTEIN

Pyrococcus woesei

UniProt P62001

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–191 Chain B; UniProt 1–191 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;50% SATURATED AMMONIUM SULFATE, 0.1 M TRIS PH 7.5, 0.1 M KCL Resolution 2.20 Å R-free 0.300

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBP_PYRWO
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–191; UniProt 1–191 Author chain B; PDBConstruct 1–191; UniProt 1–191

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 1pcz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1pcz
Deposition date deposition_date1996-10-04
Structure title titleSTRUCTURE OF TATA-BINDING PROTEIN
Keywords keywordsTRANSCRIPTION REGULATION, DNA-BINDING PROTEIN, NUCLEAR PROTEIN, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.43
Radius of gyration Rg (electron density) rg_electron24.03
Forward intensity I(0) i024843800.00
Molecular weight molecular_weight40552.0 kDa
Excluded volume excluded_volume51834 ų
Envelope volume envelope_volume59317 ų
Hydration-shell volume shell_volume22111 ų
Envelope diameter envelope_diameter92.4
Shell Rg shell_rg29.54
Envelope Rg envelope_rg24.34
Shape Rg shape_rg24.02
Total Rg total_rg24.77
Total atoms total_atoms2852
Residues n_residues366
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 dmax88.3
Rg (real space) rg_real24.65
Rg uncertainty (real space) rg_real_error0.81
I(0) (real space) i0_real2.4840e+07
I(0) uncertainty (real space) i0_real_error3.6940e+05
Rg (reciprocal space) rg_reciprocal24.60
I(0) (reciprocal space) i0_reciprocal24840000.0000
Solution quality estimate total_estimate0.8148
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.8
Skewness Skewness skewness0.610
Kurtosis Kurtosis kurtosis0.049
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9552000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.649; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.672; Smooth: 0.973

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1pcza1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.129 — TBP-like
Superfamily Superfamily superfamilyd.129.1 — TATA-box binding protein-like
Family Family familyd.129.1.1 — TATA-box binding protein (TBP), C-terminal domain
Domain ID domain_idd1pcza2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.129 — TBP-like
Superfamily Superfamily superfamilyd.129.1 — TATA-box binding protein-like
Family Family familyd.129.1.1 — TATA-box binding protein (TBP), C-terminal domain
Domain ID domain_idd1pczb1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.129 — TBP-like
Superfamily Superfamily superfamilyd.129.1 — TATA-box binding protein-like
Family Family familyd.129.1.1 — TATA-box binding protein (TBP), C-terminal domain
Domain ID domain_idd1pczb2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.129 — TBP-like
Superfamily Superfamily superfamilyd.129.1 — TATA-box binding protein-like
Family Family familyd.129.1.1 — TATA-box binding protein (TBP), C-terminal domain

CATH v4.4 (4 domains)

Domain ID domain_id1pczA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology310 — TATA-Binding Protein
Homologous superfamily homologous superfamily10 — TATA-Binding Protein
Domain ID domain_id1pczA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology310 — TATA-Binding Protein
Homologous superfamily homologous superfamily10 — TATA-Binding Protein
Domain ID domain_id1pczB01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology310 — TATA-Binding Protein
Homologous superfamily homologous superfamily10 — TATA-Binding Protein
Domain ID domain_id1pczB02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology310 — TATA-Binding Protein
Homologous superfamily homologous superfamily10 — TATA-Binding Protein

8. Citations (1)

9. Files and Curves (10)