5fwe

JMJD2A COMPLEXED WITH NI(II), NOG AND HISTONE H4(1-15)R3me2s PEPTIDE

Method: X-RAY DIFFRACTION Dmax: 94.8 Å Quality: GOOD

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

LYSINE-SPECIFIC DEMETHYLASE 4A

HOMO SAPIENS

UniProt O75164

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 1–359 Fragment:CATALYTIC DOMAIN SYNTHETIC PEPTIDE × 1 (P62805) NI NICKEL (II) ION × 1 ZN ZINC ION × 1 CL CHLORIDE ION × 1 OGA N-OXALYLGLYCINE × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;SITTING DROPS, 277 K, 0.15 M POTASSIUM BROMIDE, 30 % W/V PEG 2000 MME, pH 7.5 Resolution 2.05 Å R-free 0.255
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–359 Fragment:CATALYTIC DOMAIN SYNTHETIC PEPTIDE × 1 (P62805) NI NICKEL (II) ION × 1 ZN ZINC ION × 1 CL CHLORIDE ION × 1 OGA N-OXALYLGLYCINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;SITTING DROPS, 277 K, 0.15 M POTASSIUM BROMIDE, 30 % W/V PEG 2000 MME, pH 7.5 Resolution 2.05 Å R-free 0.255

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.

88 other PDB entries and 235 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KDM4A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 23–381; UniProt 1–359 Author chain B; PDBConstruct 23–381; UniProt 1–359

SYNTHETIC PEPTIDE

OrganismNot specified

UniProt P62805

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 D; UniProt 2–16 Fragment:HISTONE H4(1-15)R3ME2S PEPTIDE, UNP RESIDUES 2-16 Non-standard monomer:Yes (specific site not provided by mmCIF) LYSINE-SPECIFIC DEMETHYLASE 4A × 1 (O75164) NI NICKEL (II) ION × 1 ZN ZINC ION × 1 CL CHLORIDE ION × 1 OGA N-OXALYLGLYCINE × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;SITTING DROPS, 277 K, 0.15 M POTASSIUM BROMIDE, 30 % W/V PEG 2000 MME, pH 7.5 Resolution 2.05 Å R-free 0.255
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 2–16 Fragment:HISTONE H4(1-15)R3ME2S PEPTIDE, UNP RESIDUES 2-16 Non-standard monomer:Yes (specific site not provided by mmCIF) LYSINE-SPECIFIC DEMETHYLASE 4A × 1 (O75164) NI NICKEL (II) ION × 1 ZN ZINC ION × 1 CL CHLORIDE ION × 1 OGA N-OXALYLGLYCINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;SITTING DROPS, 277 K, 0.15 M POTASSIUM BROMIDE, 30 % W/V PEG 2000 MME, pH 7.5 Resolution 2.05 Å R-free 0.255

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.

581 other PDB entries and 632 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–15; UniProt 2–16 Author chain D; 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 5fwe

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5fwe
Deposition date deposition_date2016-02-15
Structure title titleJMJD2A COMPLEXED WITH NI(II), NOG AND HISTONE H4(1-15)R3me2s PEPTIDE
Keywords keywords;JMJD2A, OXIDOREDUCTASE, NON-HEME, IRON, 2-OXOGLUTARATE, DIOXYGENASE, OXYGENASE, DOUBLE-STRANDED BETA HELIX, DSBH, FACIAL TRIAD, DEMETHYLASE, HISTONE, JMJC DOMAIN, METAL BINDING PROTEIN, EPIGENETIC AND TRANSCRIPTION REGULATION, CHROMATIN REGULATOR, HYDROXYLATION ;; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.64
Radius of gyration Rg (electron density) rg_electron28.85
Forward intensity I(0) i0100624000.00
Molecular weight molecular_weight80428.0 kDa
Excluded volume excluded_volume100860 ų
Envelope volume envelope_volume122430 ų
Hydration-shell volume shell_volume35117 ų
Envelope diameter envelope_diameter99.9
Shell Rg shell_rg36.30
Envelope Rg envelope_rg28.85
Shape Rg shape_rg28.81
Total Rg total_rg29.69
Total atoms total_atoms5672
Residues n_residues704
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 dmax94.8
Rg (real space) rg_real29.64
Rg uncertainty (real space) rg_real_error0.57
I(0) (real space) i0_real1.0060e+08
I(0) uncertainty (real space) i0_real_error1.4350e+06
Rg (reciprocal space) rg_reciprocal29.64
I(0) (reciprocal space) i0_reciprocal100600000.0000
Solution quality estimate total_estimate0.8984
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.4
Skewness Skewness skewness0.311
Kurtosis Kurtosis kurtosis-0.532
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha28560000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.919; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.926

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id5fweA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily650 — Cupin
Domain ID domain_id5fweB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily650 — Cupin

8. Citations (1)

9. Files and Curves (10)