4tvq

CCM3 in complex with CCM2 LD-like motif

Method: X-RAY DIFFRACTION Dmax: 98.0 Å Quality: GOOD

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

Cerebral cavernous malformations 3 protein

Homo sapiens

UniProt Q9BUL8

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–212 Chain B; UniProt 1–212 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;15-20% PEG3350, 0.1-0.2M POTASSIUM FLUORIDE, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K Resolution 2.80 Å R-free 0.277
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–212 Chain D; UniProt 1–212 Not recorded Cerebral cavernous malformations 2 protein × 1 (Q9BSQ5) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;15-20% PEG3350, 0.1-0.2M POTASSIUM FLUORIDE, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K Resolution 2.80 Å R-free 0.277

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 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PDC10_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–214; UniProt 1–212 Author chain B; PDBConstruct 3–214; UniProt 1–212 Author chain C; PDBConstruct 3–214; UniProt 1–212 Author chain D; PDBConstruct 3–214; UniProt 1–212

Cerebral cavernous malformations 2 protein

OrganismNot specified

UniProt Q9BSQ5

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 224–239 Fragment:INTERDOMAIN LINKER LD-LIKE MOTIF RESIDUES 224-239 Cerebral cavernous malformations 3 protein × 2 (Q9BUL8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;15-20% PEG3350, 0.1-0.2M POTASSIUM FLUORIDE, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K Resolution 2.80 Å R-free 0.277

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.

7 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CCM2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–16; UniProt 224–239

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 4tvq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4tvq
Deposition date deposition_date2014-06-27
Structure title titleCCM3 in complex with CCM2 LD-like motif
Keywords keywordsFAT-HOMOLOGY DOMAIN, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.07
Radius of gyration Rg (electron density) rg_electron30.19
Forward intensity I(0) i0107747000.00
Molecular weight molecular_weight84912.0 kDa
Excluded volume excluded_volume107780 ų
Envelope volume envelope_volume142240 ų
Hydration-shell volume shell_volume39397 ų
Envelope diameter envelope_diameter105.9
Shell Rg shell_rg37.16
Envelope Rg envelope_rg30.18
Shape Rg shape_rg30.21
Total Rg total_rg30.79
Total atoms total_atoms5969
Residues n_residues735
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 dmax98.0
Rg (real space) rg_real30.98
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real1.0770e+08
I(0) uncertainty (real space) i0_real_error1.7380e+06
Rg (reciprocal space) rg_reciprocal31.02
I(0) (reciprocal space) i0_reciprocal107800000.0000
Solution quality estimate total_estimate0.8988
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary40.4
Skewness Skewness skewness0.252
Kurtosis Kurtosis kurtosis-0.361
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha34470000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.925; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.904

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id4tvqB01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology12 — Lyase 2-enoyl-coa Hydratase; Chain A, domain 2
Homologous superfamily homologous superfamily70
Domain ID domain_id4tvqB02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily330 — Nucleotidyltransferases domain 2
Domain ID domain_id4tvqD01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology12 — Lyase 2-enoyl-coa Hydratase; Chain A, domain 2
Homologous superfamily homologous superfamily70
Domain ID domain_id4tvqD02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily330 — Nucleotidyltransferases domain 2

8. Citations (1)

9. Files and Curves (10)