2c5l

Structure of PLC epsilon Ras association domain with hRas

Method: X-RAY DIFFRACTION Dmax: 102.7 Å Quality: GOOD

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

GTPASE HRAS

HOMO SAPIENS

UniProt P01112

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 1–166 Mutation:YES PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C PLC-EPSILON × 1 (Q9HBX6) GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 GOL GLYCEROL × 3 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.90 Å R-free 0.228
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–166 Mutation:YES PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C PLC-EPSILON × 1 (Q9HBX6) GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.90 Å R-free 0.228

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.

242 other PDB entries and 323 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RASH_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 8–173; UniProt 1–166 Author chain B; PDBConstruct 8–173; UniProt 1–166

PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C PLC-EPSILON

HOMO SAPIENS

UniProt Q9HBX6

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 C; UniProt 2131–2246 Fragment:RA2 DOMAIN, RESIDUES 2131-2246 Mutation:YES GTPASE HRAS × 1 (P01112) GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 GOL GLYCEROL × 3 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.90 Å R-free 0.228
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 2131–2246 Fragment:RA2 DOMAIN, RESIDUES 2131-2246 Mutation:YES GTPASE HRAS × 1 (P01112) GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.90 Å R-free 0.228

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q9HBX6_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 2–117; UniProt 2131–2246 Author chain D; PDBConstruct 2–117; UniProt 2131–2246

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 2c5l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2c5l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2c5l
Deposition date deposition_date2005-10-27
Structure title titleStructure of PLC epsilon Ras association domain with hRas
Keywords keywords;SIGNALING PROTEIN-COMPLEX, RAS, UBIQUITIN SUPERFOLD, ONCOGENE, GTP-BINDING, NUCLEOTIDE- BINDING, SIGNALING PROTEIN, DISEASE MUTATION, LIPOPROTEIN, PALMITATE, PRENYLATION, PROTO-ONCOGENE ;; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.74
Radius of gyration Rg (electron density) rg_electron28.83
Forward intensity I(0) i058979100.00
Molecular weight molecular_weight59064.0 kDa
Excluded volume excluded_volume73342 ų
Envelope volume envelope_volume92220 ų
Hydration-shell volume shell_volume28368 ų
Envelope diameter envelope_diameter107.7
Shell Rg shell_rg33.75
Envelope Rg envelope_rg29.53
Shape Rg shape_rg28.82
Total Rg total_rg29.28
Total atoms total_atoms4139
Residues n_residues510
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 dmax102.7
Rg (real space) rg_real29.01
Rg uncertainty (real space) rg_real_error0.95
I(0) (real space) i0_real5.8980e+07
I(0) uncertainty (real space) i0_real_error9.8200e+05
Rg (reciprocal space) rg_reciprocal28.89
I(0) (reciprocal space) i0_reciprocal58970000.0000
Solution quality estimate total_estimate0.7972
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary28.0
Skewness Skewness skewness0.649
Kurtosis Kurtosis kurtosis0.063
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11860000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.658; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.638; Smooth: 0.747

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd2c5la_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins
Domain ID domain_idd2c5lb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins
Domain ID domain_idd2c5lc1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.5 — Ras-binding domain, RBD
Domain ID domain_idd2c5ld_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.5 — Ras-binding domain, RBD

CATH v4.4 (4 domains)

Domain ID domain_id2c5lA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id2c5lB00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id2c5lC01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Domain ID domain_id2c5lD01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

8. Citations (1)

9. Files and Curves (10)