5xwr

Crystal Structure of RBBP4-peptide complex

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–425 Chain B; UniProt 1–425 Not recorded MET-SER-ARG-ARG-LYS-GLN-ALA-LYS-PRO-GLN-HIS-ILE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;0.1M Bis-Tris, pH5.5, 25% PEG 3,350 Resolution 2.69 Å R-free 0.256

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 69 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 19–443; UniProt 1–425 Author chain B; PDBConstruct 19–443; UniProt 1–425

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 5xwr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5xwr
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5xwr
Deposition date deposition_date2017-06-30
Structure title titleCrystal Structure of RBBP4-peptide complex
Keywords keywordsHistone Binding protein, Sall4, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.82
Radius of gyration Rg (electron density) rg_electron29.26
Forward intensity I(0) i0122003000.00
Molecular weight molecular_weight85570.0 kDa
Excluded volume excluded_volume106040 ų
Envelope volume envelope_volume130100 ų
Hydration-shell volume shell_volume36938 ų
Envelope diameter envelope_diameter108.9
Shell Rg shell_rg36.60
Envelope Rg envelope_rg29.74
Shape Rg shape_rg29.28
Total Rg total_rg29.84
Total atoms total_atoms6045
Residues n_residues775
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_real29.89
Rg uncertainty (real space) rg_real_error0.81
I(0) (real space) i0_real1.2200e+08
I(0) uncertainty (real space) i0_real_error1.8770e+06
Rg (reciprocal space) rg_reciprocal29.86
I(0) (reciprocal space) i0_reciprocal122000000.0000
Solution quality estimate total_estimate0.8634
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.0
Skewness Skewness skewness0.438
Kurtosis Kurtosis kurtosis-0.329
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha45630000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.763; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.949; Smooth: 0.981

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id5xwrA00
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_id5xwrB00
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)