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1s4z

HP1 chromo shadow domain in complex with PXVXL motif of CAF-1

Method: SOLUTION NMR Dmax: 77.6 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Chromobox protein homolog 1

Mus musculus

UniProt P23197

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count Chain A； UniProt 104–176 Chain B； UniProt 104–176 Fragment：chromo shadow domain Chromatin assembly factor 1 subunit A × 1 （Q9QWF0） SOLUTION NMR NMR measurement conditions：pH 7.5；298 K；Ionic strength (raw mmCIF value) 150mM；Pressure 1 NMR measurement conditions：pH 7.5；298 K；Ionic strength (raw mmCIF value) 150mM；Pressure 1 NMR sample composition：15N-labelled and 13C,15N labelled material complexed with unlabelled peptide | H2O NMR sample composition：15N labelled peptide complexed with unlabelled protein | H2O Resolution not provided

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.

Other PDB Difference from Current Entry 1S4Z Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1GUW STRUCTURE OF THE CHROMODOMAIN FROM MOUSE HP1beta IN COMPLEX WITH THE LYSINE 9-METHYL HISTONE H3 N-TERMINAL PEPTIDE, NMR, 25 STRUCTURES Deposited 2002-02-01 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 10–80（71 aa） Fragment：CHROMODOMAIN, RESIDUES 8 - 80
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.5；298 K；Pressure 1
NMR sample composition 150 mM NACL, 20 mM PHOSPHATE BUFFER, 10% D2O
Resolution not provided

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

View Construct and Data Evidence
UniProt name CBX1_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 3–75； UniProt 104–176 Author chain B； PDBConstruct 3–75； UniProt 104–176

Chromatin assembly factor 1 subunit A

Mus musculus

UniProt Q9QWF0

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count Chain C； UniProt 210–238 Fragment：Chromatin Assembly Factor 1 Chromobox protein homolog 1 × 2 （P23197） SOLUTION NMR NMR measurement conditions：pH 7.5；298 K；Ionic strength (raw mmCIF value) 150mM；Pressure 1 NMR measurement conditions：pH 7.5；298 K；Ionic strength (raw mmCIF value) 150mM；Pressure 1 NMR sample composition：15N-labelled and 13C,15N labelled material complexed with unlabelled peptide | H2O NMR sample composition：15N labelled peptide complexed with unlabelled protein | H2O Resolution not provided

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 CAFA_MOUSE
Isoform —
PDB entities 2
Chains and sequence ranges Author chain C； PDBConstruct 2–30； UniProt 210–238

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 1s4z

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1s4z
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1s4z
Deposition date deposition_date2004-01-19
Structure title titleHP1 chromo shadow domain in complex with PXVXL motif of CAF-1
Keywords keywordsGENE REGULATION; GENE REGULATION
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier20.49 Å
Radius of gyration Rg (electron density) rg_electron19.83 Å
Forward intensity I(0) i03554580000.00
Molecular weight molecular_weight508230.0 kDa
Excluded volume excluded_volume635880 ų
Envelope volume envelope_volume71172 ų
Hydration-shell volume shell_volume24207 ų
Envelope diameter envelope_diameter84.5 Å
Shell Rg shell_rg32.14 Å
Envelope Rg envelope_rg25.86 Å
Shape Rg shape_rg19.79 Å
Total Rg total_rg20.15 Å
Total atoms total_atoms71025
Residues n_residues4500
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax77.6 Å
Rg (real space) rg_real20.66 Å
Rg uncertainty (real space) rg_real_error0.71 Å
I(0) (real space) i0_real3.5550e+09
I(0) uncertainty (real space) i0_real_error5.3220e+07
Rg (reciprocal space) rg_reciprocal20.63 Å
I(0) (reciprocal space) i0_reciprocal3555000000.0000
Solution quality estimate total_estimate0.7930
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.9 Å
Skewness Skewness skewness0.581
Kurtosis Kurtosis kurtosis-0.033
Angular range angular_range— – 0.3900 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1836000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.572; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.609; Smooth: 0.979
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1s4za1
Class classb — All beta proteins
Fold Fold foldb.34 — SH3-like barrel
Superfamily Superfamily superfamilyb.34.13 — Chromo domain-like
Family Family familyb.34.13.2 — Chromo domain
Domain ID domain_idd1s4za2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd1s4zb1
Class classb — All beta proteins
Fold Fold foldb.34 — SH3-like barrel
Superfamily Superfamily superfamilyb.34.13 — Chromo domain-like
Family Family familyb.34.13.2 — Chromo domain
Domain ID domain_idd1s4zb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id1s4zA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily40 —
Domain ID domain_id1s4zB00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily40 —
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8. Citations (1)

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9. Files and Curves (10)