1bor

TRANSCRIPTION FACTOR PML, A PROTO-ONCOPROTEIN, NMR, 1 REPRESENTATIVE STRUCTURE AT PH 7.5, 30 C, IN THE PRESENCE OF ZINC

Method: SOLUTION NMR Dmax: 35.8 Å Quality: REASONABLE

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

TRANSCRIPTION FACTOR PML

Homo sapiens

UniProt P29590

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 49–104 Fragment:RING FINGER DOMAIN, RESIDUES 49 - 104 ZN ZINC ION × 2 SOLUTION NMR NMR measurement conditions:pH 7.5;303 K 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 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PML_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–56; UniProt 49–104

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 1bor

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1bor
Deposition date deposition_date1995-09-27
Structure title titleTRANSCRIPTION FACTOR PML, A PROTO-ONCOPROTEIN, NMR, 1 REPRESENTATIVE STRUCTURE AT PH 7.5, 30 C, IN THE PRESENCE OF ZINC
Keywords keywordsPROTO-ONCOGENE, NUCLEAR BODIES (PODS), LEUKEMIA, TRANSCRIPTION REGULATION; TRANSCRIPTION REGULATION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier11.03
Radius of gyration Rg (electron density) rg_electron9.73
Forward intensity I(0) i01024570.00
Molecular weight molecular_weight6237.0 kDa
Excluded volume excluded_volume7584 ų
Envelope volume envelope_volume7897 ų
Hydration-shell volume shell_volume7033 ų
Envelope diameter envelope_diameter33.3
Shell Rg shell_rg15.08
Envelope Rg envelope_rg10.36
Shape Rg shape_rg9.76
Total Rg total_rg11.10
Total atoms total_atoms423
Residues n_residues56
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 dmax35.8
Rg (real space) rg_real10.98
Rg uncertainty (real space) rg_real_error0.20
I(0) (real space) i0_real1.0250e+06
I(0) uncertainty (real space) i0_real_error9.8510e+03
Rg (reciprocal space) rg_reciprocal10.98
I(0) (reciprocal space) i0_reciprocal1025000.0000
Solution quality estimate total_estimate0.7446
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary13.6
Skewness Skewness skewness0.191
Kurtosis Kurtosis kurtosis-0.303
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha152400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.864; Stabil: 1.000; Sysdev: 0.368; Positv: 1.000; Valcen: 1.000; Smooth: 0.981

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_idd1bora_
Class classg — Small proteins
Fold Fold foldg.44 — RING/U-box
Superfamily Superfamily superfamilyg.44.1 — RING/U-box
Family Family familyg.44.1.1 — RING finger domain, C3HC4

CATH v4.4 (1 domains)

Domain ID domain_id1borA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology40 — Herpes Virus-1
Homologous superfamily homologous superfamily10 — Zinc/RING finger domain, C3HC4 (zinc finger)

8. Citations (2)

9. Files and Curves (10)