1sps

BINDING OF A HIGH AFFINITY PHOSPHOTYROSYL PEPTIDE TO THE SRC SH2 DOMAIN: CRYSTAL STRUCTURES OF THE COMPLEXED AND PEPTIDE-FREE FORMS

Method: X-RAY DIFFRACTION Dmax: 115.8 Å Quality: SUSPICIOUS

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

SRC SH2 DOMAIN

Rous sarcoma virus

UniProt P00524

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 144–247 Not recorded PEPTIDE YEEI × 1 (P03079) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.70 Å
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 144–247 Not recorded PEPTIDE YEEI × 1 (P03079) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.70 Å
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 144–247 Not recorded PEPTIDE YEEI × 1 (P03079) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.70 Å

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.

10 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SRC_RSVSA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–104; UniProt 144–247 Author chain B; PDBConstruct 1–104; UniProt 144–247 Author chain C; PDBConstruct 1–104; UniProt 144–247

PEPTIDE YEEI

Hamster polyomavirus

UniProt P03079

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 D; UniProt 321–331 Non-standard monomer:Yes (specific site not provided by mmCIF) SRC SH2 DOMAIN × 1 (P00524) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.70 Å
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 321–331 Non-standard monomer:Yes (specific site not provided by mmCIF) SRC SH2 DOMAIN × 1 (P00524) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.70 Å
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 321–331 Non-standard monomer:Yes (specific site not provided by mmCIF) SRC SH2 DOMAIN × 1 (P00524) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.70 Å

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TAMI_POVHA
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–11; UniProt 321–331 Author chain E; PDBConstruct 1–11; UniProt 321–331 Author chain F; PDBConstruct 1–11; UniProt 321–331

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 1sps

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1sps
Deposition date deposition_date1993-03-05
Structure title titleBINDING OF A HIGH AFFINITY PHOSPHOTYROSYL PEPTIDE TO THE SRC SH2 DOMAIN: CRYSTAL STRUCTURES OF THE COMPLEXED AND PEPTIDE-FREE FORMS
Keywords keywordsTRANSFERASE(PHOSPHOTRANSFERASE); TRANSFERASE(PHOSPHOTRANSFERASE)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier36.02
Radius of gyration Rg (electron density) rg_electron36.06
Forward intensity I(0) i024441000.00
Molecular weight molecular_weight38506.0 kDa
Excluded volume excluded_volume47856 ų
Envelope volume envelope_volume70897 ų
Hydration-shell volume shell_volume17416 ų
Envelope diameter envelope_diameter114.9
Shell Rg shell_rg39.90
Envelope Rg envelope_rg34.57
Shape Rg shape_rg36.07
Total Rg total_rg36.36
Total atoms total_atoms3353
Residues n_residues329
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 dmax115.8
Rg (real space) rg_real36.32
Rg uncertainty (real space) rg_real_error1.25
I(0) (real space) i0_real2.4440e+07
I(0) uncertainty (real space) i0_real_error4.1570e+05
Rg (reciprocal space) rg_reciprocal36.14
I(0) (reciprocal space) i0_reciprocal24440000.0000
Solution quality estimate total_estimate0.4274
Solution quality rating solution_quality SUSPICIOUS a SUSPICIOUS solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.4
Skewness Skewness skewness0.182
Kurtosis Kurtosis kurtosis-1.171
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1302000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.097; Stabil: 1.000; Sysdev: 0.101; Positv: 1.000; Valcen: 0.119; Smooth: 0.839

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1spsa_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.93 — SH2-like
Superfamily Superfamily superfamilyd.93.1 — SH2 domain
Family Family familyd.93.1.1 — SH2 domain
Domain ID domain_idd1spsb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.93 — SH2-like
Superfamily Superfamily superfamilyd.93.1 — SH2 domain
Family Family familyd.93.1.1 — SH2 domain
Domain ID domain_idd1spsc_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.93 — SH2-like
Superfamily Superfamily superfamilyd.93.1 — SH2 domain
Family Family familyd.93.1.1 — SH2 domain

CATH v4.4 (3 domains)

Domain ID domain_id1spsA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology505 — SHC Adaptor Protein
Homologous superfamily homologous superfamily10 — SH2 domain
Domain ID domain_id1spsB00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology505 — SHC Adaptor Protein
Homologous superfamily homologous superfamily10 — SH2 domain
Domain ID domain_id1spsC00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology505 — SHC Adaptor Protein
Homologous superfamily homologous superfamily10 — SH2 domain

8. Citations (1)

9. Files and Curves (10)