2xu7

Structural basis for RbAp48 binding to FOG-1

Method: X-RAY DIFFRACTION Dmax: 102.8 Å Quality: GOOD

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

HISTONE-BINDING PROTEIN RBBP4

HOMO SAPIENS

UniProt Q09028

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 1–425 Not recorded ZINC FINGER PROTEIN ZFPM1 × 1 (Q8IX07) PG4 TETRAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;20% (W/V) PEG 3350, 0.2 M NA-MALONATE PH 7.0 Resolution 1.90 Å R-free 0.225
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–425 Not recorded ZINC FINGER PROTEIN ZFPM1 × 1 (Q8IX07) PG4 TETRAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;20% (W/V) PEG 3350, 0.2 M NA-MALONATE PH 7.0 Resolution 1.90 Å R-free 0.225

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.

49 other PDB entries and 68 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBBP4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–425; UniProt 1–425 Author chain B; PDBConstruct 1–425; UniProt 1–425

ZINC FINGER PROTEIN ZFPM1

OrganismNot specified

UniProt Q8IX07

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 D; UniProt 1–15 Fragment:RBAP48-BINDING FRAGMENT, RESIDUES 1-15 HISTONE-BINDING PROTEIN RBBP4 × 1 (Q09028) PG4 TETRAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;20% (W/V) PEG 3350, 0.2 M NA-MALONATE PH 7.0 Resolution 1.90 Å R-free 0.225
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–15 Fragment:RBAP48-BINDING FRAGMENT, RESIDUES 1-15 HISTONE-BINDING PROTEIN RBBP4 × 1 (Q09028) PG4 TETRAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;20% (W/V) PEG 3350, 0.2 M NA-MALONATE PH 7.0 Resolution 1.90 Å R-free 0.225

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name FOG1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–15; UniProt 1–15 Author chain D; PDBConstruct 1–15; UniProt 1–15

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 2xu7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2xu7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2xu7
Deposition date deposition_date2010-10-15
Structure title titleStructural basis for RbAp48 binding to FOG-1
Keywords keywordsTRANSCRIPTION, CHROMATIN REMODELLING, HISTONE CHAPERONE, COREPRESSOR, GATA1-MEDIATED REPRESSION, NURD COMPLEX; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.47
Radius of gyration Rg (electron density) rg_electron29.03
Forward intensity I(0) i0115566000.00
Molecular weight molecular_weight84178.0 kDa
Excluded volume excluded_volume104780 ų
Envelope volume envelope_volume127090 ų
Hydration-shell volume shell_volume36520 ų
Envelope diameter envelope_diameter102.5
Shell Rg shell_rg36.30
Envelope Rg envelope_rg29.31
Shape Rg shape_rg29.05
Total Rg total_rg29.62
Total atoms total_atoms5947
Residues n_residues752
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 dmax102.8
Rg (real space) rg_real29.54
Rg uncertainty (real space) rg_real_error0.66
I(0) (real space) i0_real1.1560e+08
I(0) uncertainty (real space) i0_real_error1.6310e+06
Rg (reciprocal space) rg_reciprocal29.51
I(0) (reciprocal space) i0_reciprocal115600000.0000
Solution quality estimate total_estimate0.7830
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary30.5
Skewness Skewness skewness0.436
Kurtosis Kurtosis kurtosis-0.339
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha44850000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.740; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.955; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id2xu7A00
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id2xu7B00
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)