8tx8

Crystal Structure of RBBP4 bound to ZNF512B peptide

Method: X-RAY DIFFRACTION Dmax: 104.7 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 512B × 1 (Q96KM6) FMT FORMIC ACID × 3 EDO 1,2-ETHANEDIOL × 7 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;Condition Morpheus G2 0.1 M MES/imidazole, pH 6.5, 40% v/v ethylene glycol; 20 % w/v PEG 8000, 0.1 M mixture of carboxylic acids Resolution 2.20 Å R-free 0.244
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 512B × 1 (Q96KM6) FMT FORMIC ACID × 3 EDO 1,2-ETHANEDIOL × 4 ACT ACETATE ION × 1 OXM OXAMIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;Condition Morpheus G2 0.1 M MES/imidazole, pH 6.5, 40% v/v ethylene glycol; 20 % w/v PEG 8000, 0.1 M mixture of carboxylic acids Resolution 2.20 Å R-free 0.244

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 21–445; UniProt 1–425 Author chain B; PDBConstruct 21–445; UniProt 1–425

Zinc finger protein 512B

OrganismNot specified

UniProt Q96KM6

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 419–430 Non-standard monomer:Yes (specific site not provided by mmCIF) Histone-binding protein RBBP4 × 1 (Q09028) FMT FORMIC ACID × 3 EDO 1,2-ETHANEDIOL × 7 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;Condition Morpheus G2 0.1 M MES/imidazole, pH 6.5, 40% v/v ethylene glycol; 20 % w/v PEG 8000, 0.1 M mixture of carboxylic acids Resolution 2.20 Å R-free 0.244
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 419–430 Non-standard monomer:Yes (specific site not provided by mmCIF) Histone-binding protein RBBP4 × 1 (Q09028) FMT FORMIC ACID × 3 EDO 1,2-ETHANEDIOL × 4 ACT ACETATE ION × 1 OXM OXAMIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;Condition Morpheus G2 0.1 M MES/imidazole, pH 6.5, 40% v/v ethylene glycol; 20 % w/v PEG 8000, 0.1 M mixture of carboxylic acids Resolution 2.20 Å R-free 0.244

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Z512B_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 2–13; UniProt 419–430 Author chain D; PDBConstruct 2–13; UniProt 419–430

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 8tx8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8tx8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8tx8
Deposition date deposition_date2023-08-22
Structure title titleCrystal Structure of RBBP4 bound to ZNF512B peptide
Keywords keywordsNuRD, chromatin compaction, zinc finger, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.24
Radius of gyration Rg (electron density) rg_electron29.79
Forward intensity I(0) i0128801000.00
Molecular weight molecular_weight88747.0 kDa
Excluded volume excluded_volume110380 ų
Envelope volume envelope_volume133120 ų
Hydration-shell volume shell_volume37392 ų
Envelope diameter envelope_diameter111.6
Shell Rg shell_rg36.81
Envelope Rg envelope_rg30.11
Shape Rg shape_rg29.79
Total Rg total_rg30.37
Total atoms total_atoms6263
Residues n_residues773
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 dmax104.7
Rg (real space) rg_real30.34
Rg uncertainty (real space) rg_real_error1.03
I(0) (real space) i0_real1.2880e+08
I(0) uncertainty (real space) i0_real_error2.1960e+06
Rg (reciprocal space) rg_reciprocal30.30
I(0) (reciprocal space) i0_reciprocal128800000.0000
Solution quality estimate total_estimate0.8518
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.2
Skewness Skewness skewness0.459
Kurtosis Kurtosis kurtosis-0.306
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha48400000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.749; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.908; Smooth: 0.913

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)