2xyi

Crystal Structure of Nurf55 in complex with a H4 peptide

Method: X-RAY DIFFRACTION Dmax: 70.7 Å Quality: GOOD

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

PROBABLE HISTONE-BINDING PROTEIN CAF1

DROSOPHILA MELANOGASTER

UniProt Q24572

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 1–430 Not recorded HISTONE H4 × 1 (P84040) PG4 TETRAETHYLENE GLYCOL × 3 PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;35%(V/V) PEG 400, 100MM MES PH 6 Resolution 1.75 Å R-free 0.195

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.

4 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CAF1_DROME
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–430; UniProt 1–430

HISTONE H4

OrganismNot specified

UniProt P84040

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 27–46 Fragment:RESIDUES 27-46 PROBABLE HISTONE-BINDING PROTEIN CAF1 × 1 (Q24572) PG4 TETRAETHYLENE GLYCOL × 3 PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;35%(V/V) PEG 400, 100MM MES PH 6 Resolution 1.75 Å R-free 0.195

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.

18 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_DROME
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–20; UniProt 27–46

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 2xyi

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2xyi
Deposition date deposition_date2010-11-17
Structure title titleCrystal Structure of Nurf55 in complex with a H4 peptide
Keywords keywordsTRANSCRIPTION, REPRESSOR, PHOSPHOPROTEIN, WD-REPEAT; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.11
Radius of gyration Rg (electron density) rg_electron20.96
Forward intensity I(0) i035887200.00
Molecular weight molecular_weight45503.0 kDa
Excluded volume excluded_volume56601 ų
Envelope volume envelope_volume65879 ų
Hydration-shell volume shell_volume25423 ų
Envelope diameter envelope_diameter73.8
Shell Rg shell_rg28.53
Envelope Rg envelope_rg21.40
Shape Rg shape_rg20.93
Total Rg total_rg21.95
Total atoms total_atoms3211
Residues n_residues393
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 dmax70.7
Rg (real space) rg_real21.97
Rg uncertainty (real space) rg_real_error0.30
I(0) (real space) i0_real3.5890e+07
I(0) uncertainty (real space) i0_real_error4.2210e+05
Rg (reciprocal space) rg_reciprocal22.00
I(0) (reciprocal space) i0_reciprocal35890000.0000
Solution quality estimate total_estimate0.8923
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.4
Skewness Skewness skewness0.191
Kurtosis Kurtosis kurtosis-0.420
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8193000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.880; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.959

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_id2xyiA00
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase

8. Citations (1)

9. Files and Curves (10)