9mez

Crystal structure of MRAS(GDP) bound to LZTR1(Kelch domain)

Method: X-RAY DIFFRACTION Dmax: 211.1 Å Quality: REASONABLE

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

Ras-related protein M-Ras

Homo sapiens

UniProt O14807

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 1–181 Not recorded Leucine-zipper-like transcriptional regulator 1 × 1 (Q8N653) GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 FMT FORMIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;277 K;11.2% w/v PEG3350, 5.26% Tacsimate pH 6.0 Resolution 2.80 Å R-free 0.255
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–181 Not recorded Leucine-zipper-like transcriptional regulator 1 × 1 (Q8N653) GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 MLA MALONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;277 K;11.2% w/v PEG3350, 5.26% Tacsimate pH 6.0 Resolution 2.80 Å R-free 0.255
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 1–181 Not recorded Leucine-zipper-like transcriptional regulator 1 × 1 (Q8N653) GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 MLA MALONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;277 K;11.2% w/v PEG3350, 5.26% Tacsimate pH 6.0 Resolution 2.80 Å R-free 0.255
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 1–181 Not recorded Leucine-zipper-like transcriptional regulator 1 × 1 (Q8N653) GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 MLA MALONIC ACID × 1 ACT ACETATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;277 K;11.2% w/v PEG3350, 5.26% Tacsimate pH 6.0 Resolution 2.80 Å R-free 0.255
5 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain I; UniProt 1–181 Not recorded Leucine-zipper-like transcriptional regulator 1 × 1 (Q8N653) GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;277 K;11.2% w/v PEG3350, 5.26% Tacsimate pH 6.0 Resolution 2.80 Å R-free 0.255

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.

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

View Construct and Data Evidence
UniProt name RASM_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–182; UniProt 1–181 Author chain C; PDBConstruct 2–182; UniProt 1–181 Author chain E; PDBConstruct 2–182; UniProt 1–181 Author chain G; PDBConstruct 2–182; UniProt 1–181 Author chain I; PDBConstruct 2–182; UniProt 1–181

Leucine-zipper-like transcriptional regulator 1

Homo sapiens

UniProt Q8N653

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 50–331 Chain B; UniProt 384–422 Not recorded Ras-related protein M-Ras × 1 (O14807) GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 FMT FORMIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;277 K;11.2% w/v PEG3350, 5.26% Tacsimate pH 6.0 Resolution 2.80 Å R-free 0.255
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 50–331 Chain D; UniProt 384–422 Not recorded Ras-related protein M-Ras × 1 (O14807) GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 MLA MALONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;277 K;11.2% w/v PEG3350, 5.26% Tacsimate pH 6.0 Resolution 2.80 Å R-free 0.255
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 50–331 Chain F; UniProt 384–422 Not recorded Ras-related protein M-Ras × 1 (O14807) GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 MLA MALONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;277 K;11.2% w/v PEG3350, 5.26% Tacsimate pH 6.0 Resolution 2.80 Å R-free 0.255
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 50–331 Chain H; UniProt 384–422 Not recorded Ras-related protein M-Ras × 1 (O14807) GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 MLA MALONIC ACID × 1 ACT ACETATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;277 K;11.2% w/v PEG3350, 5.26% Tacsimate pH 6.0 Resolution 2.80 Å R-free 0.255
5 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain J; UniProt 50–331 Chain J; UniProt 384–422 Not recorded Ras-related protein M-Ras × 1 (O14807) GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;277 K;11.2% w/v PEG3350, 5.26% Tacsimate pH 6.0 Resolution 2.80 Å R-free 0.255

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 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LZTR1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–283; UniProt 50–331 Author chain B; PDBConstruct 284–322; UniProt 384–422 Author chain D; PDBConstruct 2–283; UniProt 50–331 Author chain D; PDBConstruct 284–322; UniProt 384–422 Author chain F; PDBConstruct 2–283; UniProt 50–331 Author chain F; PDBConstruct 284–322; UniProt 384–422 Author chain H; PDBConstruct 2–283; UniProt 50–331 Author chain H; PDBConstruct 284–322; UniProt 384–422 Author chain J; PDBConstruct 2–283; UniProt 50–331 Author chain J; PDBConstruct 284–322; UniProt 384–422

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 9mez

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9mez
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9mez
Deposition date deposition_date2024-12-09
Structure title titleCrystal structure of MRAS(GDP) bound to LZTR1(Kelch domain)
Keywords keywordsSubstrate adaptor, ONCOPROTEIN; ONCOPROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier65.06
Radius of gyration Rg (electron density) rg_electron67.10
Forward intensity I(0) i01103700000.00
Molecular weight molecular_weight275810.0 kDa
Excluded volume excluded_volume343420 ų
Envelope volume envelope_volume505800 ų
Hydration-shell volume shell_volume71858 ų
Envelope diameter envelope_diameter235.3
Shell Rg shell_rg53.43
Envelope Rg envelope_rg66.39
Shape Rg shape_rg67.10
Total Rg total_rg66.79
Total atoms total_atoms19463
Residues n_residues2444
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 dmax211.1
Rg (real space) rg_real66.55
Rg uncertainty (real space) rg_real_error2.11
I(0) (real space) i0_real1.1030e+09
I(0) uncertainty (real space) i0_real_error2.3220e+07
Rg (reciprocal space) rg_reciprocal63.67
I(0) (reciprocal space) i0_reciprocal1098000000.0000
Solution quality estimate total_estimate0.5544
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary44.0
Skewness Skewness skewness0.640
Kurtosis Kurtosis kurtosis-0.355
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0007
Highest regularization parameter α highest_alpha37410000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.684; Stabil: 0.999; Sysdev: 0.013; Positv: 1.000; Valcen: 0.666; Smooth: 0.449

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)