4pc0

Structure of the human RbAp48-MTA1(670-711) complex

Method: X-RAY DIFFRACTION Dmax: 106.3 Å Quality: REASONABLE

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 Metastasis-associated protein MTA1 × 1 (Q13330) GOL GLYCEROL × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.2 M calcium acetate and 20% w/v PEG 3350 Resolution 2.50 Å R-free 0.259
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: Dimeric(2) Consistent with protein copy count Chain B; UniProt 1–425 Not recorded Metastasis-associated protein MTA1 × 1 (Q13330) CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.2 M calcium acetate and 20% w/v PEG 3350 Resolution 2.50 Å R-free 0.259

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

Metastasis-associated protein MTA1

OrganismNot specified

UniProt Q13330

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 C; UniProt 653–694 Fragment:Residues 653-694 Histone-binding protein RBBP4 × 1 (Q09028) GOL GLYCEROL × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.2 M calcium acetate and 20% w/v PEG 3350 Resolution 2.50 Å R-free 0.259
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: Dimeric(2) Consistent with protein copy count Chain D; UniProt 653–694 Fragment:Residues 653-694 Histone-binding protein RBBP4 × 1 (Q09028) CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.2 M calcium acetate and 20% w/v PEG 3350 Resolution 2.50 Å R-free 0.259

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.

9 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MTA1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–42; UniProt 653–694 Author chain D; PDBConstruct 1–42; UniProt 653–694

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 4pc0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4pc0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4pc0
Deposition date deposition_date2014-04-14
Structure title titleStructure of the human RbAp48-MTA1(670-711) complex
Keywords keywordsCell cycle, MTA1-NuRD subcomplex; CELL CYCLE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.95
Radius of gyration Rg (electron density) rg_electron32.56
Forward intensity I(0) i0148639000.00
Molecular weight molecular_weight95370.0 kDa
Excluded volume excluded_volume118340 ų
Envelope volume envelope_volume154980 ų
Hydration-shell volume shell_volume40135 ų
Envelope diameter envelope_diameter111.5
Shell Rg shell_rg39.06
Envelope Rg envelope_rg32.06
Shape Rg shape_rg32.54
Total Rg total_rg33.12
Total atoms total_atoms6734
Residues n_residues846
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 dmax106.3
Rg (real space) rg_real32.99
Rg uncertainty (real space) rg_real_error0.77
I(0) (real space) i0_real1.4860e+08
I(0) uncertainty (real space) i0_real_error2.4190e+06
Rg (reciprocal space) rg_reciprocal32.98
I(0) (reciprocal space) i0_reciprocal148600000.0000
Solution quality estimate total_estimate0.6735
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary33.2
Skewness Skewness skewness0.325
Kurtosis Kurtosis kurtosis-0.553
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha55330000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.915; Stabil: 1.000; Sysdev: 0.049; Positv: 1.000; Valcen: 0.968; Smooth: 0.890

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id4pc0A00
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_id4pc0B00
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)