6f4m

Human JMJD5 in its apo form.

Method: X-RAY DIFFRACTION Dmax: 60.8 Å Quality: GOOD

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

JmjC domain-containing protein 5

Homo sapiens

UniProt Q8N371

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 182–416 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;298 K;0.1 M Bis-Tris pH 6.5, 22.5 % PEG3350, 0.002 M MnCl2, 300 nl sitting drops (sample:well, 1:1 ratio) Resolution 1.71 Å R-free 0.186

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.

25 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KDM8_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–235; UniProt 182–416

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 6f4m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6f4m
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6f4m
Deposition date deposition_date2017-11-29
Structure title titleHuman JMJD5 in its apo form.
Keywords keywords;OXIDOREDUCTASE, NON-HEME, IRON, 2-OXOGLUTARATE, DIOXYGENASE, JMJC, JMJC DOMAIN, Lysine-specific demethylase 8, JmjC domain-containing protein 5, Arginyl C-3 Hydroxylase, JMJD5, KDM8, OXYGENASE, HYPOXIA, DNA-BINDING, METAL-BINDING, TRANSLATION, DSBH, FACIAL TRIAD, CYTOPLASM, JMJC HYDROXYLASE, JMJC DEMETHYLASE, KDMS, POST-TRANSLATIONAL MODIFICATIONS, PTM, BETA-HYDROXYLATION, HYDROXYLATION, ARGININE HYDROXYLATION, RCC1 domain-containing protein 1, RCCD1, Regulator of chromosome condensation, 40S ribosomal protein S6, RPS6, RIBOSOME BIOGENESIS, TRANSCRIPTION, EPIGENETIC REGULATION, SIGNALING, DEVELOPMENT, CELL STRUCTURE, TRANSCRIPTION ACTIVATOR/INHIBITOR, PHOSPHORYLATION, CANCER, POLYMORPHISM ;; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.01
Radius of gyration Rg (electron density) rg_electron17.76
Forward intensity I(0) i011822200.00
Molecular weight molecular_weight26766.0 kDa
Excluded volume excluded_volume33881 ų
Envelope volume envelope_volume38700 ų
Hydration-shell volume shell_volume18210 ų
Envelope diameter envelope_diameter60.2
Shell Rg shell_rg23.99
Envelope Rg envelope_rg17.91
Shape Rg shape_rg17.72
Total Rg total_rg18.83
Total atoms total_atoms3740
Residues n_residues235
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 dmax60.8
Rg (real space) rg_real18.89
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real1.1820e+07
I(0) uncertainty (real space) i0_real_error1.4260e+05
Rg (reciprocal space) rg_reciprocal18.91
I(0) (reciprocal space) i0_reciprocal11820000.0000
Solution quality estimate total_estimate0.8926
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.6
Skewness Skewness skewness0.143
Kurtosis Kurtosis kurtosis-0.447
Angular range angular_range— – 0.4200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2521000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.871; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id6f4mA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily650 — Cupin

8. Citations (1)

9. Files and Curves (10)