2b2t

Tandem chromodomains of human CHD1 complexed with Histone H3 Tail containing trimethyllysine 4 and phosphothreonine 3

Method: X-RAY DIFFRACTION Dmax: 89.6 Å Quality: GOOD

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

Chromodomain-helicase-DNA-binding protein 1

Homo sapiens

UniProt O14646

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 268–443 Chain B; UniProt 268–443 Chain C; UniProt 268–373 Fragment:residues 268-443 Mutation:C436M Non-standard monomer:Yes (specific site not provided by mmCIF) Fragment:residues 268-373 Non-standard monomer:Yes (specific site not provided by mmCIF) Histone H3 tail × 1 (P68431) X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;283 K;4% PEG3350, 0.05M HEPES, pH 8.0, 10mM BTP, 12.5mM NaCl, 5mM TCEP, VAPOR DIFFUSION, HANGING DROP, temperature 283K, pH 8.00 Resolution 2.45 Å R-free 0.266

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.

17 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CHD1_HUMAN
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 10–185; UniProt 268–443 Author chain B; PDBConstruct 10–185; UniProt 268–443 Author chain C; PDBConstruct 10–115; UniProt 268–373

Histone H3 tail

OrganismNot specified

UniProt P68431

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 D; UniProt 1–19 Fragment:residues 1-19 Non-standard monomer:Yes (specific site not provided by mmCIF) Chromodomain-helicase-DNA-binding protein 1 × 2 (O14646) Chromodomain-helicase-DNA-binding protein 1 × 1 (O14646) X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;283 K;4% PEG3350, 0.05M HEPES, pH 8.0, 10mM BTP, 12.5mM NaCl, 5mM TCEP, VAPOR DIFFUSION, HANGING DROP, temperature 283K, pH 8.00 Resolution 2.45 Å R-free 0.266

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.

402 other PDB entries and 475 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H31_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–19; UniProt 1–19

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 2b2t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2b2t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2b2t
Deposition date deposition_date2005-09-19
Structure title titleTandem chromodomains of human CHD1 complexed with Histone H3 Tail containing trimethyllysine 4 and phosphothreonine 3
Keywords keywords;CHD, Chromodomain, three stranded antiparallel Beta sheet, alpha helix linker, histone H3, trimethyllysine, phosphothreonine, PEPTIDE BINDING PROTEIN ;; PEPTIDE BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.87
Radius of gyration Rg (electron density) rg_electron25.19
Forward intensity I(0) i048062400.00
Molecular weight molecular_weight51607.0 kDa
Excluded volume excluded_volume63582 ų
Envelope volume envelope_volume82212 ų
Hydration-shell volume shell_volume27966 ų
Envelope diameter envelope_diameter95.6
Shell Rg shell_rg31.50
Envelope Rg envelope_rg25.22
Shape Rg shape_rg25.18
Total Rg total_rg25.91
Total atoms total_atoms3610
Residues n_residues431
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 dmax89.6
Rg (real space) rg_real25.87
Rg uncertainty (real space) rg_real_error0.87
I(0) (real space) i0_real4.8060e+07
I(0) uncertainty (real space) i0_real_error7.7330e+05
Rg (reciprocal space) rg_reciprocal25.87
I(0) (reciprocal space) i0_reciprocal48060000.0000
Solution quality estimate total_estimate0.8405
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.3
Skewness Skewness skewness0.375
Kurtosis Kurtosis kurtosis-0.137
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8638000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.740; Stabil: 0.990; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.756

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (7 domains)

Domain ID domain_idd2b2ta1
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_idd2b2ta2
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_idd2b2ta3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2b2tb1
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_idd2b2tb2
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_idd2b2tb3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2b2tc1
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

CATH v4.4 (5 domains)

Domain ID domain_id2b2tA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily40
Domain ID domain_id2b2tA02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily40
Domain ID domain_id2b2tB01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily40
Domain ID domain_id2b2tB02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily40
Domain ID domain_id2b2tC00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily40

8. Citations (1)

9. Files and Curves (10)