3ktf

Structure of the N-terminal BRCT domain of human microcephalin (MCPH1).

Method: X-RAY DIFFRACTION Dmax: 82.0 Å Quality: GOOD

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

Microcephalin

Homo sapiens

UniProt Q8NEM0

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 1–101 Non-standard monomer:Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;295 K;0.2M sodium succinate, 15% PEG 3350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 1.60 Å R-free 0.195
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–101 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;295 K;0.2M sodium succinate, 15% PEG 3350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 1.60 Å R-free 0.195
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 1–101 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;295 K;0.2M sodium succinate, 15% PEG 3350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 1.60 Å R-free 0.195

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.

8 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MCPH1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–103; UniProt 1–101 Author chain B; PDBConstruct 3–103; UniProt 1–101 Author chain C; PDBConstruct 3–103; UniProt 1–101

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 3ktf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3ktf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3ktf
Deposition date deposition_date2009-11-25
Structure title titleStructure of the N-terminal BRCT domain of human microcephalin (MCPH1).
Keywords keywords;BRCT DOMAIN, MCPH1, MICROCEPHALIN, Cytoplasm, Cytoskeleton, Dwarfism, Mental retardation, Phosphoprotein, Polymorphism, Primary microcephaly, CELL CYCLE ;; CELL CYCLE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.39
Radius of gyration Rg (electron density) rg_electron23.84
Forward intensity I(0) i017075900.00
Molecular weight molecular_weight31698.0 kDa
Excluded volume excluded_volume39806 ų
Envelope volume envelope_volume50357 ų
Hydration-shell volume shell_volume18889 ų
Envelope diameter envelope_diameter82.3
Shell Rg shell_rg29.23
Envelope Rg envelope_rg23.77
Shape Rg shape_rg23.78
Total Rg total_rg24.73
Total atoms total_atoms2222
Residues n_residues278
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 dmax82.0
Rg (real space) rg_real24.52
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real1.7080e+07
I(0) uncertainty (real space) i0_real_error2.7260e+05
Rg (reciprocal space) rg_reciprocal24.49
I(0) (reciprocal space) i0_reciprocal17080000.0000
Solution quality estimate total_estimate0.8705
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.1
Skewness Skewness skewness0.369
Kurtosis Kurtosis kurtosis-0.519
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3448000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.863; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.740; Smooth: 0.984

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id3ktfA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily10190 — BRCT domain
Domain ID domain_id3ktfB00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily10190 — BRCT domain
Domain ID domain_id3ktfC00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily10190 — BRCT domain

8. Citations (1)

9. Files and Curves (10)