2bze

NMR Structure of human RTF1 PLUS3 domain.

Method: SOLUTION NMR Dmax: 49.1 Å Quality: REASONABLE

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

KIAA0252 PROTEIN

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 A; UniProt 228–359 Fragment:PLUS3, RESIDUES 228-359 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6;298 K;Ionic strength (raw mmCIF value) 200;Pressure 1.0 NMR sample composition:90% WATER/10% D2O Resolution not provided

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 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q92541_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 22–153; UniProt 228–359

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 2bze

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2bze
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2bze
Deposition date deposition_date2005-08-16
Structure title titleNMR Structure of human RTF1 PLUS3 domain.
Keywords keywords;HUMAN RTF1 PLUS3 DOMAIN, TRANSCRIPTION, ELONGATION, PAF1 COMPLEX, HISTONE H3 METHYLATION, H2B UBIQUITINATION, CDC73, LEO1, CTR9, PLUS3 DOMAIN, TRANSCRIPTION REGULATION, STRUCTURAL PROTEOMICS IN EUROPE, SPINE, STRUCTURAL GENOMICS ;; TRANSCRIPTION REGULATION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier17.86
Radius of gyration Rg (electron density) rg_electron17.16
Forward intensity I(0) i02806810000.00
Molecular weight molecular_weight437700.0 kDa
Excluded volume excluded_volume543310 ų
Envelope volume envelope_volume76328 ų
Hydration-shell volume shell_volume25633 ų
Envelope diameter envelope_diameter83.4
Shell Rg shell_rg32.04
Envelope Rg envelope_rg27.49
Shape Rg shape_rg17.16
Total Rg total_rg17.39
Total atoms total_atoms61275
Residues n_residues3825
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 dmax49.1
Rg (real space) rg_real16.64
Rg uncertainty (real space) rg_real_error0.09
I(0) (real space) i0_real2.6700e+09
I(0) uncertainty (real space) i0_real_error2.6130e+07
Rg (reciprocal space) rg_reciprocal18.06
I(0) (reciprocal space) i0_reciprocal2807000000.0000
Solution quality estimate total_estimate0.6726
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.2
Skewness Skewness skewness0.367
Kurtosis Kurtosis kurtosis-0.172
Angular range angular_range— – 0.4450 −1
Current regularization parameter α current_alpha2.7790
Highest regularization parameter α highest_alpha625800.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.003; Oscil: 0.930; Stabil: 0.986; Sysdev: 0.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2bzea1
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_idd2bzea2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id2bzeA01
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)