4l1p

Crystal Structure of Human Rtf1 Plus3 domain

Method: X-RAY DIFFRACTION Dmax: 68.9 Å Quality: EXCELLENT

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

RNA polymerase-associated protein RTF1 homolog

Homo sapiens

UniProt Q92541

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 B; UniProt 353–484 Fragment:UNP residues 353-484 GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;Trisodium citrate, PEG 3000, pH 5.5, vapor diffusion, sitting drop, temperature 293K Resolution 2.12 Å R-free 0.240
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 353–484 Fragment:UNP residues 353-484 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;Trisodium citrate, PEG 3000, pH 5.5, vapor diffusion, sitting drop, temperature 293K Resolution 2.12 Å R-free 0.240

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.

17 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RTF1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 7–138; UniProt 353–484 Author chain B; PDBConstruct 7–138; UniProt 353–484

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 4l1p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4l1p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4l1p
Deposition date deposition_date2013-06-03
Structure title titleCrystal Structure of Human Rtf1 Plus3 domain
Keywords keywordsTutor, Plus3, Peptide binding protein, Spt5 CTR binding, Transcription, Paf1 complex, Rtf1, ORF association region, Chromatin; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.04
Radius of gyration Rg (electron density) rg_electron21.12
Forward intensity I(0) i016281300.00
Molecular weight molecular_weight30474.0 kDa
Excluded volume excluded_volume38238 ų
Envelope volume envelope_volume47249 ų
Hydration-shell volume shell_volume19025 ų
Envelope diameter envelope_diameter68.2
Shell Rg shell_rg26.91
Envelope Rg envelope_rg21.21
Shape Rg shape_rg21.10
Total Rg total_rg21.99
Total atoms total_atoms4283
Residues n_residues259
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 dmax68.9
Rg (real space) rg_real22.01
Rg uncertainty (real space) rg_real_error0.41
I(0) (real space) i0_real1.6280e+07
I(0) uncertainty (real space) i0_real_error2.0100e+05
Rg (reciprocal space) rg_reciprocal22.02
I(0) (reciprocal space) i0_reciprocal16280000.0000
Solution quality estimate total_estimate0.9074
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.6
Skewness Skewness skewness0.254
Kurtosis Kurtosis kurtosis-0.612
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3798000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.938; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.993

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd4l1pa1
Class classb — All beta proteins
Fold Fold foldb.34 — SH3-like barrel
Superfamily Superfamily superfamilyb.34.21 — Plus3-like
Family Family familyb.34.21.1 — Plus3
Domain ID domain_idd4l1pa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd4l1pb1
Class classb — All beta proteins
Fold Fold foldb.34 — SH3-like barrel
Superfamily Superfamily superfamilyb.34.21 — Plus3-like
Family Family familyb.34.21.1 — Plus3
Domain ID domain_idd4l1pb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id4l1pA00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology70 — Cathepsin B; Chain A
Homologous superfamily homologous superfamily200 — Plus-3 domain
Domain ID domain_id4l1pB00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology70 — Cathepsin B; Chain A
Homologous superfamily homologous superfamily200 — Plus-3 domain

8. Citations (1)

9. Files and Curves (10)