1c02

CRYSTAL STRUCTURE OF YEAST YPD1P

Method: X-RAY DIFFRACTION Dmax: 83.9 Å Quality: REASONABLE

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

PHOSPHOTRANSFERASE YPD1P

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–167 Chain B; UniProt 2–167 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.36;297 K;AMMONIUM SULFATE, LITHIUM SULFATE, HEPES, PEG 400, pH 7.36, VAPOR DIFFUSION, HANGING DROP, temperature 297.0K Resolution 1.80 Å R-free 0.247

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 17 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 1–166; UniProt 2–167 Author chain B; PDBConstruct 1–166; UniProt 2–167

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 1c02

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1c02
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1c02
Deposition date deposition_date1999-07-14
Structure title titleCRYSTAL STRUCTURE OF YEAST YPD1P
Keywords keywordsHELIX-BUNDLE, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.66
Radius of gyration Rg (electron density) rg_electron22.86
Forward intensity I(0) i024821600.00
Molecular weight molecular_weight38053.0 kDa
Excluded volume excluded_volume47645 ų
Envelope volume envelope_volume57527 ų
Hydration-shell volume shell_volume21807 ų
Envelope diameter envelope_diameter88.1
Shell Rg shell_rg28.86
Envelope Rg envelope_rg23.13
Shape Rg shape_rg22.85
Total Rg total_rg23.64
Total atoms total_atoms2678
Residues n_residues332
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 dmax83.9
Rg (real space) rg_real23.72
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real2.4820e+07
I(0) uncertainty (real space) i0_real_error3.9200e+05
Rg (reciprocal space) rg_reciprocal23.71
I(0) (reciprocal space) i0_reciprocal24820000.0000
Solution quality estimate total_estimate0.6089
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.9
Skewness Skewness skewness0.416
Kurtosis Kurtosis kurtosis-0.321
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8046000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.734; Stabil: 1.000; Sysdev: 0.286; Positv: 1.000; Valcen: 0.853; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1c02a_
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_idd1c02b_
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 (2 domains)

Domain ID domain_id1c02A00
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_id1c02B00
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)