1z23

The serine-rich domain from Crk-associated substrate (p130Cas)

Method: SOLUTION NMR Dmax: 55.3 Å Quality: REASONABLE

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

CRK-associated substrate

Rattus norvegicus

UniProt Q63767

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 546–708 Fragment:serine-rich domain, SRR-B, residues 546-708 Mutation:V546G P547S No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7.9;298 K;Ionic strength (raw mmCIF value) 0.1;Pressure ambient NMR sample composition:1.8mM protein U-15N, 20mM Tris U-2H, pH 7.9, 100mM NaCl, 5mM beta-mercaptoethanol, 1mM 4-(2-aminoethyl)benzene fluoride (AEBSF), 90% H2O, 10% D2O; | 90% H2O/10% D2O NMR sample composition:1.8mM protein U-13C, U-15N, 20mM Tris U-2H, pH 7.9, 100mM NaCl, 5mM beta-mercaptoethanol, 1mM 4-(2-aminoethyl)benzene fluoride (AEBSF), 90% H2O, 10% D2O | 90% H2O/10% D2O NMR sample composition:1.8mM protein U-13C, U-15N, ~60% 2H, 20mM Tris U-2H, pH 7.9, 100mM NaCl, 5mM beta-mercaptoethanol, 1mM 4-(2-aminoethyl)benzene fluoride (AEBSF), 90% H2O, 10% D2O | 90% H2O/10% D2O NMR sample composition:1.8mM protein U-15N, ~60% 2H, 20mM Tris U-2H, pH 7.9, 100mM NaCl, 5mM beta-mercaptoethanol, 1mM 4-(2-aminoethyl)benzene fluoride (AEBSF), 90% H2O, 10% D2O | 90% H2O/10% D2O Resolution not provided

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BCA1_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–163; UniProt 546–708

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 1z23

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1z23
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1z23
Deposition date deposition_date2005-03-07
Structure title titleThe serine-rich domain from Crk-associated substrate (p130Cas)
Keywords keywordsfour-helix bundle, CELL ADHESION; CELL ADHESION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier19.92
Radius of gyration Rg (electron density) rg_electron19.70
Forward intensity I(0) i01790550000.00
Molecular weight molecular_weight346450.0 kDa
Excluded volume excluded_volume429350 ų
Envelope volume envelope_volume57671 ų
Hydration-shell volume shell_volume20692 ų
Envelope diameter envelope_diameter88.8
Shell Rg shell_rg30.73
Envelope Rg envelope_rg25.57
Shape Rg shape_rg19.71
Total Rg total_rg19.84
Total atoms total_atoms48780
Residues n_residues3260
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 dmax55.3
Rg (real space) rg_real18.80
Rg uncertainty (real space) rg_real_error0.13
I(0) (real space) i0_real1.7170e+09
I(0) uncertainty (real space) i0_real_error1.7180e+07
Rg (reciprocal space) rg_reciprocal20.21
I(0) (reciprocal space) i0_reciprocal1791000000.0000
Solution quality estimate total_estimate0.6649
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary17.9
Skewness Skewness skewness0.466
Kurtosis Kurtosis kurtosis-0.441
Angular range angular_range— – 0.4000 −1
Current regularization parameter α current_alpha2.2520
Highest regularization parameter α highest_alpha1950000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.914; Stabil: 0.991; Sysdev: 0.000; Positv: 1.000; Valcen: 0.951; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id1z23A00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily830 — Serine-rich domain

8. Citations (2)

9. Files and Curves (10)