5xfo

Structure of the N-terminal domains of PHF1

Method: X-RAY DIFFRACTION Dmax: 84.5 Å Quality: GOOD

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

PHD finger protein 1

Homo sapiens

UniProt O43189

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 25–340 Fragment:UNP residues 25-340 ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;0.1M Tris-pH 8.0, 10% PEG 3350, 22% ethylene glycerol Resolution 1.90 Å R-free 0.227

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.

8 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PHF1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–316; UniProt 25–340

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 5xfo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5xfo
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5xfo
Deposition date deposition_date2017-04-11
Structure title titleStructure of the N-terminal domains of PHF1
Keywords keywordsPHF1, PCL1, PRC2, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.48
Radius of gyration Rg (electron density) rg_electron22.87
Forward intensity I(0) i023518200.00
Molecular weight molecular_weight36074.0 kDa
Excluded volume excluded_volume44782 ų
Envelope volume envelope_volume54996 ų
Hydration-shell volume shell_volume21066 ų
Envelope diameter envelope_diameter87.2
Shell Rg shell_rg28.73
Envelope Rg envelope_rg23.11
Shape Rg shape_rg22.88
Total Rg total_rg23.59
Total atoms total_atoms2513
Residues n_residues315
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 dmax84.5
Rg (real space) rg_real23.59
Rg uncertainty (real space) rg_real_error0.65
I(0) (real space) i0_real2.3520e+07
I(0) uncertainty (real space) i0_real_error2.7070e+05
Rg (reciprocal space) rg_reciprocal23.56
I(0) (reciprocal space) i0_reciprocal23520000.0000
Solution quality estimate total_estimate0.8424
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.7
Skewness Skewness skewness0.483
Kurtosis Kurtosis kurtosis-0.199
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4453000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.712; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.828; Smooth: 0.983

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id5xfoA02
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 (1)

9. Files and Curves (10)