1upl

Crystal structure of MO25 alpha

Method: X-RAY DIFFRACTION Dmax: 141.4 Å Quality: REASONABLE

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

MO25 PROTEIN

HOMO SAPIENS

UniProt Q9Y376

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 1–341 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;15 % PEG 20000, 0.1 M MES PH 6.5, 4.4 % GAMMA BUTYROLACTONE Resolution 2.60 Å R-free 0.280
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–341 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;15 % PEG 20000, 0.1 M MES PH 6.5, 4.4 % GAMMA BUTYROLACTONE Resolution 2.60 Å R-free 0.280

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 MO25_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–341; UniProt 1–341 Author chain B; PDBConstruct 1–341; UniProt 1–341

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 1upl

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1upl
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1upl
Deposition date deposition_date2003-10-07
Structure title titleCrystal structure of MO25 alpha
Keywords keywordsTRANSFERASE, STRAD, LKB1, ARMADILLO; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier41.73
Radius of gyration Rg (electron density) rg_electron41.86
Forward intensity I(0) i077480200.00
Molecular weight molecular_weight73262.0 kDa
Excluded volume excluded_volume92240 ų
Envelope volume envelope_volume130850 ų
Hydration-shell volume shell_volume27520 ų
Envelope diameter envelope_diameter138.2
Shell Rg shell_rg43.96
Envelope Rg envelope_rg40.92
Shape Rg shape_rg41.83
Total Rg total_rg42.09
Total atoms total_atoms5107
Residues n_residues604
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 dmax141.4
Rg (real space) rg_real42.10
Rg uncertainty (real space) rg_real_error2.10
I(0) (real space) i0_real7.7480e+07
I(0) uncertainty (real space) i0_real_error1.5940e+06
Rg (reciprocal space) rg_reciprocal41.74
I(0) (reciprocal space) i0_reciprocal77450000.0000
Solution quality estimate total_estimate0.7337
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary22.3
Skewness Skewness skewness0.342
Kurtosis Kurtosis kurtosis-0.851
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4108000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.494; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.395; Smooth: 0.658

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1upla_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.15 — Mo25 protein
Domain ID domain_idd1uplb_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.15 — Mo25 protein

CATH v4.4 (2 domains)

Domain ID domain_id1uplA00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant
Domain ID domain_id1uplB00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant

8. Citations (1)

9. Files and Curves (10)