1ydl

Crystal Structure of the Human TFIIH, Northeast Structural Genomics Target HR2045.

Method: X-RAY DIFFRACTION Dmax: 59.7 Å Quality: GOOD

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

general transcription factor IIH, polypeptide 5

Homo sapiens

UniProt Q6ZYL4

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–71 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;22% PEG 3350, 100 mM MgCl2, and 10 mM DTT, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.30 Å R-free 0.297

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.

52 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TF2H5_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–79; UniProt 1–71

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 1ydl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1ydl
Deposition date deposition_date2004-12-24
Structure title titleCrystal Structure of the Human TFIIH, Northeast Structural Genomics Target HR2045.
Keywords keywords;alpha-beta protein, Structural Genomics, PSI, Protein Structure Initiative, Northeast Structural Genomics Consortium, NESG, TRANSCRIPTION ;; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.18
Radius of gyration Rg (electron density) rg_electron15.30
Forward intensity I(0) i01532150.00
Molecular weight molecular_weight8207.0 kDa
Excluded volume excluded_volume10180 ų
Envelope volume envelope_volume12983 ų
Hydration-shell volume shell_volume8387 ų
Envelope diameter envelope_diameter59.3
Shell Rg shell_rg18.91
Envelope Rg envelope_rg16.10
Shape Rg shape_rg15.36
Total Rg total_rg16.00
Total atoms total_atoms565
Residues n_residues68
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 dmax59.7
Rg (real space) rg_real16.35
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real1.5320e+06
I(0) uncertainty (real space) i0_real_error1.9490e+04
Rg (reciprocal space) rg_reciprocal16.33
I(0) (reciprocal space) i0_reciprocal1532000.0000
Solution quality estimate total_estimate0.8233
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.8
Skewness Skewness skewness0.531
Kurtosis Kurtosis kurtosis-0.115
Angular range angular_range— – 0.4900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha133300.0000
Real-space data points n_real_points79
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.669; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.714; Smooth: 0.977

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1ydla1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.295 — TFB5-like
Superfamily Superfamily superfamilyd.295.1 — TFB5-like
Family Family familyd.295.1.1 — TFB5-like

CATH v4.4 (1 domains)

Domain ID domain_id1ydlA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily1220 — TFB5-like

8. Citations (1)

9. Files and Curves (10)