2rnw

The Structural Basis for Site-Specific Lysine-Acetylated Histone Recognition by the Bromodomains of the Human Transcriptional Co-Activators PCAf and CBP

Method: SOLUTION NMR Dmax: 42.7 Å Quality: REASONABLE

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

Histone acetyltransferase PCAF

Homo sapiens

UniProt Q92831

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 719–832 Fragment:UNP residues 719-832 Histone H3 × 1 (P61830) SOLUTION NMR NMR measurement conditions:pH 6.5;298 K;Pressure ambient NMR sample composition:0.5 mM [U-100% 13C; U-100% 15N] potassium phosphate, 90% H2O/10% D2O | 90% H2O/10% D2O 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.

24 other PDB entries and 39 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PCAF_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–118; UniProt 719–832

Histone H3

Saccharomyces cerevisiae

UniProt P61830

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 B; UniProt 2–16 Fragment:UNP residues 2-16 Non-standard monomer:Yes (specific site not provided by mmCIF) Histone acetyltransferase PCAF × 1 (Q92831) SOLUTION NMR NMR measurement conditions:pH 6.5;298 K;Pressure ambient NMR sample composition:0.5 mM [U-100% 13C; U-100% 15N] potassium phosphate, 90% H2O/10% D2O | 90% H2O/10% D2O 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.

37 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H3_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–15; UniProt 2–16

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 2rnw

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2rnw
Deposition date deposition_date2008-02-03
Structure title titleThe Structural Basis for Site-Specific Lysine-Acetylated Histone Recognition by the Bromodomains of the Human Transcriptional Co-Activators PCAf and CBP
Keywords keywords;bromodomain, histone, acetyltransferase, Acyltransferase, Cell cycle, Host-virus interaction, Nucleus, Polymorphism, Transcription, Transcription regulation, Acetylation, Chromosomal protein, DNA damage, DNA repair, DNA-binding, Methylation, Nucleosome core, Phosphoprotein, TRANSFERASE-NUCLEAR PROTEIN COMPLEX ;; TRANSFERASE/NUCLEAR PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.93
Radius of gyration Rg (electron density) rg_electron15.50
Forward intensity I(0) i01311650000.00
Molecular weight molecular_weight312860.0 kDa
Excluded volume excluded_volume394000 ų
Envelope volume envelope_volume43933 ų
Hydration-shell volume shell_volume18252 ų
Envelope diameter envelope_diameter77.9
Shell Rg shell_rg27.25
Envelope Rg envelope_rg22.13
Shape Rg shape_rg15.46
Total Rg total_rg15.87
Total atoms total_atoms44220
Residues n_residues2640
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 dmax42.7
Rg (real space) rg_real14.90
Rg uncertainty (real space) rg_real_error0.07
I(0) (real space) i0_real1.2470e+09
I(0) uncertainty (real space) i0_real_error1.0560e+07
Rg (reciprocal space) rg_reciprocal16.08
I(0) (reciprocal space) i0_reciprocal1312000000.0000
Solution quality estimate total_estimate0.6804
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary16.7
Skewness Skewness skewness0.352
Kurtosis Kurtosis kurtosis-0.352
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha3.3390
Highest regularization parameter α highest_alpha672200.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.006; Oscil: 0.962; Stabil: 0.986; Sysdev: 0.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2rnwa2
Class classa — All alpha proteins
Fold Fold folda.29 — Bromodomain-like
Superfamily Superfamily superfamilya.29.2 — Bromodomain
Family Family familya.29.2.1 — Bromodomain
Domain ID domain_idd2rnwa3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id2rnwA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology920 — Histone Acetyltransferase; Chain A
Homologous superfamily homologous superfamily10 — Bromodomain-like

8. Citations (1)

9. Files and Curves (10)