4cco

60S ribosomal protein L8 histidine hydroxylase (NO66 S373C) in complex with Mn(II), N-oxalylglycine (NOG) and 60S ribosomal protein L8 (RPL8 G214C) peptide fragment (complex-3)

Method: X-RAY DIFFRACTION Dmax: 117.5 Å Quality: GOOD

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

BIFUNCTIONAL LYSINE-SPECIFIC DEMETHYLASE AND HISTIDYL-HYDROXYLASE NO66

HOMO SAPIENS

UniProt Q9H6W3

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 183–641 Chain B; UniProt 183–641 Fragment:CATALYTIC DOMAIN, RESIDUES 183-641 60S RIBOSOMAL PROTEIN L8 × 4 (P62917) MN MANGANESE (II) ION × 4 OGA N-OXALYLGLYCINE × 4 EDO 1,2-ETHANEDIOL × 10 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;VAPOR DIFFUSION, SITTING DROP 0.1M BIS-TRIS PROPANE PH 7.4, 0.36M MAGNESIUM FORMATE, 0.002M MNCL2, TEMPERATURE 293K Resolution 2.30 Å R-free 0.225

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.

9 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NO66_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–460; UniProt 183–641 Author chain B; PDBConstruct 2–460; UniProt 183–641

60S RIBOSOMAL PROTEIN L8

OrganismNot specified

UniProt P62917

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain C; UniProt 205–224 Chain D; UniProt 205–224 Fragment:RESIDUES 205-239 Mutation:YES BIFUNCTIONAL LYSINE-SPECIFIC DEMETHYLASE AND HISTIDYL-HYDROXYLASE NO66 × 4 (Q9H6W3) MN MANGANESE (II) ION × 4 OGA N-OXALYLGLYCINE × 4 EDO 1,2-ETHANEDIOL × 10 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;VAPOR DIFFUSION, SITTING DROP 0.1M BIS-TRIS PROPANE PH 7.4, 0.36M MAGNESIUM FORMATE, 0.002M MNCL2, TEMPERATURE 293K Resolution 2.30 Å R-free 0.225

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.

159 other PDB entries and 159 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL8_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–20; UniProt 205–224 Author chain D; PDBConstruct 1–20; UniProt 205–224

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 4cco

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4cco
Deposition date deposition_date2013-10-23
Structure title title60S ribosomal protein L8 histidine hydroxylase (NO66 S373C) in complex with Mn(II), N-oxalylglycine (NOG) and 60S ribosomal protein L8 (RPL8 G214C) peptide fragment (complex-3)
Keywords keywords;OXIDOREDUCTASE, NON-HEME, IRON-BINDING, DSBH, 2-OXOGLUTARATE, DIOXYGENASE, JMJC DOMAIN, RIBOSOME BIOGENESIS, NUCLEAR PROTEIN, RPL8, BETA-HYDROXYLATION, TRANSCRIPTION AND EPIGENETIC REGULATION, SIGNALING ;; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier36.76
Radius of gyration Rg (electron density) rg_electron36.30
Forward intensity I(0) i0176125000.00
Molecular weight molecular_weight106750.0 kDa
Excluded volume excluded_volume133120 ų
Envelope volume envelope_volume175520 ų
Hydration-shell volume shell_volume39901 ų
Envelope diameter envelope_diameter113.7
Shell Rg shell_rg43.52
Envelope Rg envelope_rg35.73
Shape Rg shape_rg36.29
Total Rg total_rg36.79
Total atoms total_atoms7524
Residues n_residues941
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 dmax117.5
Rg (real space) rg_real36.78
Rg uncertainty (real space) rg_real_error0.92
I(0) (real space) i0_real1.7610e+08
I(0) uncertainty (real space) i0_real_error2.7910e+06
Rg (reciprocal space) rg_reciprocal36.78
I(0) (reciprocal space) i0_reciprocal176100000.0000
Solution quality estimate total_estimate0.8930
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary32.8
Skewness Skewness skewness0.206
Kurtosis Kurtosis kurtosis-0.799
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha33790000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.921; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.907; Smooth: 0.936

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id4ccoA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily650 — Cupin
Domain ID domain_id4ccoA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily1500 — JmjC domain-containing ribosomal oxygenase (ROX), dimer domain
Domain ID domain_id4ccoA03
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology930 — Outer Surface Protein A; domain 3
Homologous superfamily homologous superfamily40
Domain ID domain_id4ccoB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily650 — Cupin
Domain ID domain_id4ccoB02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily1500 — JmjC domain-containing ribosomal oxygenase (ROX), dimer domain
Domain ID domain_id4ccoB03
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology930 — Outer Surface Protein A; domain 3
Homologous superfamily homologous superfamily40

8. Citations (2)

9. Files and Curves (10)