4fzv

Crystal structure of the human MTERF4:NSUN4:SAM ternary complex

Method: X-RAY DIFFRACTION Dmax: 113.0 Å Quality: GOOD

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

Putative methyltransferase NSUN4

Homo sapiens

UniProt Q96CB9

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 A; UniProt 26–384 Non-standard monomer:Yes (specific site not provided by mmCIF) mTERF domain-containing protein 2 × 1 (Q7Z6M4) SAM S-ADENOSYLMETHIONINE × 1 FMT FORMIC ACID × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;298 K;0.15 M magnesium formate, 50 mM Bis-Tris, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K Resolution 2.00 Å R-free 0.190

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.

14 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NSUN4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–359; UniProt 26–384

mTERF domain-containing protein 2

Homo sapiens

UniProt Q7Z6M4

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 92–330 Not recorded Putative methyltransferase NSUN4 × 1 (Q96CB9) SAM S-ADENOSYLMETHIONINE × 1 FMT FORMIC ACID × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;298 K;0.15 M magnesium formate, 50 mM Bis-Tris, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K Resolution 2.00 Å R-free 0.190

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.

14 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MTER2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–239; UniProt 92–330

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 4fzv

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4fzv
Deposition date deposition_date2012-07-08
Structure title titleCrystal structure of the human MTERF4:NSUN4:SAM ternary complex
Keywords keywordsMTERF fold, methyltransferase fold, rRNA methyltransferase, mitochondria, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.50
Radius of gyration Rg (electron density) rg_electron31.26
Forward intensity I(0) i062907600.00
Molecular weight molecular_weight60994.0 kDa
Excluded volume excluded_volume75546 ų
Envelope volume envelope_volume98981 ų
Hydration-shell volume shell_volume28580 ų
Envelope diameter envelope_diameter118.3
Shell Rg shell_rg34.79
Envelope Rg envelope_rg32.80
Shape Rg shape_rg31.36
Total Rg total_rg31.24
Total atoms total_atoms4272
Residues n_residues567
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 dmax113.0
Rg (real space) rg_real32.08
Rg uncertainty (real space) rg_real_error1.28
I(0) (real space) i0_real6.2910e+07
I(0) uncertainty (real space) i0_real_error1.0390e+06
Rg (reciprocal space) rg_reciprocal31.84
I(0) (reciprocal space) i0_reciprocal62890000.0000
Solution quality estimate total_estimate0.7544
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary110.8
Skewness Skewness skewness0.710
Kurtosis Kurtosis kurtosis-0.140
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12300000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.468; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.563; Smooth: 0.836

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id4fzvA01
Class class6 — Special
Architecture architecture20 — Other non-globular
Topology topology240 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily40
Domain ID domain_id4fzvA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily150 — Vaccinia Virus protein VP39

8. Citations (1)

9. Files and Curves (10)