4eyu

The free structure of the mouse C-terminal domain of KDM6B

Method: X-RAY DIFFRACTION Dmax: 104.2 Å Quality: EXCELLENT

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

Lysine-specific demethylase 6B

Mus musculus

UniProt Q5NCY0

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1155–1293 Chain A; UniProt 1321–1641 Fragment:UNP residues 1155-1641 OGA N-OXALYLGLYCINE × 1 NI NICKEL (II) ION × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.2;298 K;11% methanol, 6% MPD, 5% PEG 4K, 5% GLYCEROL, HEPES pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.30 Å R-free 0.268
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1155–1293 Chain B; UniProt 1321–1641 Fragment:UNP residues 1155-1641 OGA N-OXALYLGLYCINE × 1 NI NICKEL (II) ION × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.2;298 K;11% methanol, 6% MPD, 5% PEG 4K, 5% GLYCEROL, HEPES pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.30 Å R-free 0.268

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.

3 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KDM6B_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–139; UniProt 1155–1293 Author chain A; PDBConstruct 166–486; UniProt 1321–1641 Author chain B; PDBConstruct 1–139; UniProt 1155–1293 Author chain B; PDBConstruct 166–486; UniProt 1321–1641

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 4eyu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4eyu
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4eyu
Deposition date deposition_date2012-05-01
Structure title titleThe free structure of the mouse C-terminal domain of KDM6B
Keywords keywordsJMJC domain, Histone K27 trimethyl and dimethyl demethylase, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.41
Radius of gyration Rg (electron density) rg_electron31.76
Forward intensity I(0) i0171909000.00
Molecular weight molecular_weight104220.0 kDa
Excluded volume excluded_volume130160 ų
Envelope volume envelope_volume167550 ų
Hydration-shell volume shell_volume43182 ų
Envelope diameter envelope_diameter114.2
Shell Rg shell_rg39.34
Envelope Rg envelope_rg31.84
Shape Rg shape_rg31.76
Total Rg total_rg32.39
Total atoms total_atoms7333
Residues n_residues909
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 dmax104.2
Rg (real space) rg_real32.31
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real1.7190e+08
I(0) uncertainty (real space) i0_real_error2.3210e+06
Rg (reciprocal space) rg_reciprocal32.36
I(0) (reciprocal space) i0_reciprocal171900000.0000
Solution quality estimate total_estimate0.9036
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary40.4
Skewness Skewness skewness0.219
Kurtosis Kurtosis kurtosis-0.505
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha54970000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.925; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.969

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id4eyuA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily650 — Cupin
Domain ID domain_id4eyuA02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily1370
Domain ID domain_id4eyuA03
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology110 — Cysteine Rich Protein
Homologous superfamily homologous superfamily20
Domain ID domain_id4eyuB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily650 — Cupin
Domain ID domain_id4eyuB02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily1370
Domain ID domain_id4eyuB03
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology110 — Cysteine Rich Protein
Homologous superfamily homologous superfamily20

8. Citations (1)

9. Files and Curves (10)