4bxf

60S ribosomal protein L27A histidine hydroxylase (MINA53 Y209C) in complex with MN(II), 2-oxoglutarate (2OG) and 60S ribosomal protein L27A (RPL27A G37C) peptide fragment

Method: X-RAY DIFFRACTION Dmax: 97.9 Å Quality: EXCELLENT

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

BIFUNCTIONAL LYSINE-SPECIFIC DEMETHYLASE AND HISTIDYL-HYDROXYLASE MINA

HOMO SAPIENS

UniProt Q8IUF8

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 26–465 Chain B; UniProt 26–465 Fragment:CATALYTIC DOMAIN, RESIDUES 26-465 Mutation:YES 60S RIBOSOMAL PROTEIN L27A × 2 (P46776) MN MANGANESE (II) ION × 2 AKG 2-OXOGLUTARIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;VAPOR DIFFUSION SITTING DROP. 0.1M BIS-TRIS PROPANE PH 8.5, 0.02M NA-K-PHOSPHATE, 20-22% (W/V) PEG 3350, 0.002 M MNCL2, TEMPERATURE 293K Resolution 2.05 Å R-free 0.221

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.

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

View Construct and Data Evidence
UniProt name MINA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–442; UniProt 26–465 Author chain B; PDBConstruct 3–442; UniProt 26–465

60S RIBOSOMAL PROTEIN L27A

OrganismNot specified

UniProt P46776

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 32–50 Chain D; UniProt 32–50 Fragment:RESIDUES 32-50 Mutation:YES BIFUNCTIONAL LYSINE-SPECIFIC DEMETHYLASE AND HISTIDYL-HYDROXYLASE MINA × 2 (Q8IUF8) MN MANGANESE (II) ION × 2 AKG 2-OXOGLUTARIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;VAPOR DIFFUSION SITTING DROP. 0.1M BIS-TRIS PROPANE PH 8.5, 0.02M NA-K-PHOSPHATE, 20-22% (W/V) PEG 3350, 0.002 M MNCL2, TEMPERATURE 293K Resolution 2.05 Å R-free 0.221

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.

172 other PDB entries and 172 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL27A_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–19; UniProt 32–50 Author chain D; PDBConstruct 1–19; UniProt 32–50

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 4bxf

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4bxf
Deposition date deposition_date2013-07-10
Structure title title60S ribosomal protein L27A histidine hydroxylase (MINA53 Y209C) in complex with MN(II), 2-oxoglutarate (2OG) and 60S ribosomal protein L27A (RPL27A G37C) peptide fragment
Keywords keywords;OXIDOREDUCTASE-TRANSLATION COMPLEX, OXIDOREDUCTASE, NON-HEME, IRON-BINDING, DSBH, DIOXYGENASE, JMJC DOMAIN, RIBOSOME BIOGENESIS, NUCLEAR PROTEIN, BETA-HYDROXYLATION, TRANSCRIPTION AND EPIGENETIC REGULATION, SIGNALING ;; OXIDOREDUCTASE/TRANSLATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.37
Radius of gyration Rg (electron density) rg_electron31.67
Forward intensity I(0) i0140631000.00
Molecular weight molecular_weight95585.0 kDa
Excluded volume excluded_volume119920 ų
Envelope volume envelope_volume154130 ų
Hydration-shell volume shell_volume39977 ų
Envelope diameter envelope_diameter102.5
Shell Rg shell_rg39.70
Envelope Rg envelope_rg30.97
Shape Rg shape_rg31.67
Total Rg total_rg32.35
Total atoms total_atoms6745
Residues n_residues864
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 dmax97.9
Rg (real space) rg_real32.22
Rg uncertainty (real space) rg_real_error0.84
I(0) (real space) i0_real1.4060e+08
I(0) uncertainty (real space) i0_real_error2.3610e+06
Rg (reciprocal space) rg_reciprocal32.29
I(0) (reciprocal space) i0_reciprocal140600000.0000
Solution quality estimate total_estimate0.9069
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.0
Skewness Skewness skewness0.105
Kurtosis Kurtosis kurtosis-0.683
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha45470000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.970; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.879

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_id4bxfA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily650 — Cupin
Domain ID domain_id4bxfA02
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_id4bxfA03
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology930 — Outer Surface Protein A; domain 3
Homologous superfamily homologous superfamily40
Domain ID domain_id4bxfB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily650 — Cupin
Domain ID domain_id4bxfB02
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_id4bxfB03
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)