1c03

CRYSTAL STRUCTURE OF YPD1P (TRICLINIC FORM)

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

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

HYPOTHETICAL PROTEIN YDL235C

Saccharomyces cerevisiae

UniProt Q07688

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 1–167 Mutation:C-TERMINAL 6 HIS-TAG No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.36;297 K;PEG 400, ammonium sulfate, Hepes, Li2SO4, pH 7.36, VAPOR DIFFUSION, HANGING DROP, temperature 297K Resolution 2.30 Å R-free 0.248
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–167 Mutation:C-TERMINAL 6 HIS-TAG No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.36;297 K;PEG 400, ammonium sulfate, Hepes, Li2SO4, pH 7.36, VAPOR DIFFUSION, HANGING DROP, temperature 297K Resolution 2.30 Å R-free 0.248
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 1–167 Mutation:C-TERMINAL 6 HIS-TAG No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.36;297 K;PEG 400, ammonium sulfate, Hepes, Li2SO4, pH 7.36, VAPOR DIFFUSION, HANGING DROP, temperature 297K Resolution 2.30 Å R-free 0.248
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 1–167 Mutation:C-TERMINAL 6 HIS-TAG No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.36;297 K;PEG 400, ammonium sulfate, Hepes, Li2SO4, pH 7.36, VAPOR DIFFUSION, HANGING DROP, temperature 297K Resolution 2.30 Å R-free 0.248

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 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q07688_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–167; UniProt 1–167 Author chain B; PDBConstruct 1–167; UniProt 1–167 Author chain C; PDBConstruct 1–167; UniProt 1–167 Author chain D; PDBConstruct 1–167; UniProt 1–167

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 1c03

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1c03
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1c03
Deposition date deposition_date1999-07-14
Structure title titleCRYSTAL STRUCTURE OF YPD1P (TRICLINIC FORM)
Keywords keywordsFOUR HELICAL BUNDLE, SIGNAL TRANSDUCTION, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.83
Radius of gyration Rg (electron density) rg_electron26.72
Forward intensity I(0) i090871100.00
Molecular weight molecular_weight74115.0 kDa
Excluded volume excluded_volume92604 ų
Envelope volume envelope_volume116470 ų
Hydration-shell volume shell_volume35201 ų
Envelope diameter envelope_diameter83.1
Shell Rg shell_rg35.12
Envelope Rg envelope_rg26.21
Shape Rg shape_rg26.72
Total Rg total_rg27.61
Total atoms total_atoms5220
Residues n_residues652
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_real27.59
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real9.0870e+07
I(0) uncertainty (real space) i0_real_error1.1000e+06
Rg (reciprocal space) rg_reciprocal27.67
I(0) (reciprocal space) i0_reciprocal90880000.0000
Solution quality estimate total_estimate0.9059
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.8
Skewness Skewness skewness0.016
Kurtosis Kurtosis kurtosis-0.575
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha28520000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.952; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.939

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1c03a_
Class classa — All alpha proteins
Fold Fold folda.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamilya.24.10 — Histidine-containing phosphotransfer domain, HPT domain
Family Family familya.24.10.2 — Phosphorelay protein-like
Domain ID domain_idd1c03b_
Class classa — All alpha proteins
Fold Fold folda.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamilya.24.10 — Histidine-containing phosphotransfer domain, HPT domain
Family Family familya.24.10.2 — Phosphorelay protein-like
Domain ID domain_idd1c03c_
Class classa — All alpha proteins
Fold Fold folda.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamilya.24.10 — Histidine-containing phosphotransfer domain, HPT domain
Family Family familya.24.10.2 — Phosphorelay protein-like
Domain ID domain_idd1c03d_
Class classa — All alpha proteins
Fold Fold folda.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamilya.24.10 — Histidine-containing phosphotransfer domain, HPT domain
Family Family familya.24.10.2 — Phosphorelay protein-like

CATH v4.4 (4 domains)

Domain ID domain_id1c03A00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily160 — HPT domain
Domain ID domain_id1c03B00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily160 — HPT domain
Domain ID domain_id1c03C00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily160 — HPT domain
Domain ID domain_id1c03D00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily160 — HPT domain

8. Citations (2)

9. Files and Curves (10)