7klr

Solution structure of the PHD1 domain of histone demethylase KDM5A in complex with a histone H3(1-10) peptide

Method: SOLUTION NMR Dmax: 39.6 Å Quality: GOOD

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

Lysine-specific demethylase 5A

Homo sapiens

UniProt P29375

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 287–344 Not recorded Histone H3.1 × 1 (P68431) ZN ZINC ION × 2 SOLUTION NMR NMR measurement conditions:pH 7.5;298 K;Ionic strength (raw mmCIF value) 150;Pressure 1 NMR sample composition:900 uM [U-13C; U-15N] Histone lysine demethylase 5A, KDM5A, 4000 uM Histone H3.1, 50 mM HEPES, 150 mM sodium chloride, 5 mM beta-mercaptoethanol, 0.1 mM ZnCl2, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:550 uM [U-13C; U-15N] Histone lysine demethylase 5A, KDM5A, 800 uM Histone H3.1, 50 mM HEPES, 150 mM sodium chloride, 5 mM beta-mercaptoethanol, 0.1 mM ZnCl2, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:1250 uM [U-13C; U-15N] Histone lysine demethylase 5A, KDM5A, 400 uM Histone H3.1, 50 mM HEPES, 150 mM sodium chloride, 5 mM beta-mercaptoethanol, 0.1 mM ZnCl2, 95% H2O/5% D2O | 95% H2O/5% 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.

45 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KDM5A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–59; UniProt 287–344

Histone H3.1

Homo sapiens

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 2–11 Not recorded Lysine-specific demethylase 5A × 1 (P29375) ZN ZINC ION × 2 SOLUTION NMR NMR measurement conditions:pH 7.5;298 K;Ionic strength (raw mmCIF value) 150;Pressure 1 NMR sample composition:900 uM [U-13C; U-15N] Histone lysine demethylase 5A, KDM5A, 4000 uM Histone H3.1, 50 mM HEPES, 150 mM sodium chloride, 5 mM beta-mercaptoethanol, 0.1 mM ZnCl2, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:550 uM [U-13C; U-15N] Histone lysine demethylase 5A, KDM5A, 800 uM Histone H3.1, 50 mM HEPES, 150 mM sodium chloride, 5 mM beta-mercaptoethanol, 0.1 mM ZnCl2, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:1250 uM [U-13C; U-15N] Histone lysine demethylase 5A, KDM5A, 400 uM Histone H3.1, 50 mM HEPES, 150 mM sodium chloride, 5 mM beta-mercaptoethanol, 0.1 mM ZnCl2, 95% H2O/5% D2O | 95% H2O/5% 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.

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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–10; UniProt 2–11

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 7klr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7klr
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7klr
Deposition date deposition_date2020-10-31
Structure title titleSolution structure of the PHD1 domain of histone demethylase KDM5A in complex with a histone H3(1-10) peptide
Keywords keywordsPHD, H3, Epigenetics, KDM5A, GENE REGULATION; GENE REGULATION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier11.81
Radius of gyration Rg (electron density) rg_electron11.86
Forward intensity I(0) i0403620000.00
Molecular weight molecular_weight157510.0 kDa
Excluded volume excluded_volume191620 ų
Envelope volume envelope_volume18334 ų
Hydration-shell volume shell_volume11562 ų
Envelope diameter envelope_diameter44.8
Shell Rg shell_rg19.32
Envelope Rg envelope_rg14.00
Shape Rg shape_rg11.88
Total Rg total_rg11.94
Total atoms total_atoms21100
Residues n_residues1380
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 dmax39.6
Rg (real space) rg_real11.77
Rg uncertainty (real space) rg_real_error0.35
I(0) (real space) i0_real4.0360e+08
I(0) uncertainty (real space) i0_real_error4.3840e+06
Rg (reciprocal space) rg_reciprocal11.77
I(0) (reciprocal space) i0_reciprocal403600000.0000
Solution quality estimate total_estimate0.7966
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.0
Skewness Skewness skewness0.211
Kurtosis Kurtosis kurtosis-0.200
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha85950.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.787; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd7klra1
Class classg — Small proteins
Fold Fold foldg.50 — FYVE/PHD zinc finger
Superfamily Superfamily superfamilyg.50.1 — FYVE/PHD zinc finger
Family Family familyg.50.1.0 — automated matches
Domain ID domain_idd7klra2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

8. Citations (1)

9. Files and Curves (10)