6iiw

Crystal structure of human UHRF1 PHD finger in complex with PAF15

Method: X-RAY DIFFRACTION Dmax: 45.8 Å Quality: GOOD

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

E3 ubiquitin-protein ligase UHRF1

Homo sapiens

UniProt Q96T88

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 299–366 Not recorded PCNA-associated factor × 1 (Q15004) ZN ZINC ION × 4 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;0.1 M HEPES (pH 7.5), 70% (v/v) MPD Resolution 1.70 Å R-free 0.189

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.

44 other PDB entries and 76 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UHRF1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–68; UniProt 299–366

PCNA-associated factor

OrganismNot specified

UniProt Q15004

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 2–11 Not recorded E3 ubiquitin-protein ligase UHRF1 × 1 (Q96T88) ZN ZINC ION × 4 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;0.1 M HEPES (pH 7.5), 70% (v/v) MPD Resolution 1.70 Å R-free 0.189

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PAF15_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–10; UniProt 2–11

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 6iiw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6iiw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6iiw
Deposition date deposition_date2018-10-07
Structure title titleCrystal structure of human UHRF1 PHD finger in complex with PAF15
Keywords keywordsDNA methylation, histone modification, replication, LIGASE; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier13.30
Radius of gyration Rg (electron density) rg_electron12.48
Forward intensity I(0) i02166480.00
Molecular weight molecular_weight8859.0 kDa
Excluded volume excluded_volume10475 ų
Envelope volume envelope_volume11897 ų
Hydration-shell volume shell_volume8600 ų
Envelope diameter envelope_diameter42.6
Shell Rg shell_rg17.51
Envelope Rg envelope_rg12.98
Shape Rg shape_rg12.46
Total Rg total_rg13.61
Total atoms total_atoms590
Residues n_residues71
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 dmax45.8
Rg (real space) rg_real13.31
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real2.1660e+06
I(0) uncertainty (real space) i0_real_error2.3570e+04
Rg (reciprocal space) rg_reciprocal13.31
I(0) (reciprocal space) i0_reciprocal2166000.0000
Solution quality estimate total_estimate0.7888
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.7
Skewness Skewness skewness0.384
Kurtosis Kurtosis kurtosis-0.126
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha192100.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.764; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.959; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id6iiwA00
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)