1ygp

PHOSPHORYLATED FORM OF YEAST GLYCOGEN PHOSPHORYLASE WITH PHOSPHATE BOUND IN THE ACTIVE SITE.

Method: X-RAY DIFFRACTION
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1. Protein Identity and Related Structures Protein Identity & Related Structures

YEAST GLYCOGEN PHOSPHORYLASE

Saccharomyces cerevisiae

UniProt P06738

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 2 PHOSPHATE ION × 4 PYRIDOXAL-5'-PHOSPHATE × 2 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name PHSG_YEAST
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 28–879; UniProt 23–901 Author chain B; PDBConstruct 28–879; UniProt 23–901

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id1ygp
Deposition date deposition_date1996-05-30
Structure title titlePHOSPHORYLATED FORM OF YEAST GLYCOGEN PHOSPHORYLASE WITH PHOSPHATE BOUND IN THE ACTIVE SITE.
Keywords keywordsYEAST, PHOSPHORYLATED FORM, GLYCOSYLTRANSFERASE; GLYCOSYLTRANSFERASE
Experimental Method methodX-RAY DIFFRACTION
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1ygp__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1ygp__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1ygp__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)38.22 Å
Rg (electron density)37.83 Å
Total Rg38.18 Å
Atom count13538
Residues1716
Excluded volume240300 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1ygp__assembly_1__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (3)

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6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1ygpa_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.87 — UDP-Glycosyltransferase/glycogen phosphorylase
Superfamily Superfamily superfamilyc.87.1 — UDP-Glycosyltransferase/glycogen phosphorylase
Family Family familyc.87.1.4 — Oligosaccharide phosphorylase
Domain ID domain_idd1ygpb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.87 — UDP-Glycosyltransferase/glycogen phosphorylase
Superfamily Superfamily superfamilyc.87.1 — UDP-Glycosyltransferase/glycogen phosphorylase
Family Family familyc.87.1.4 — Oligosaccharide phosphorylase

CATH v4.4 (4 domains)

Domain ID domain_id1ygpA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2000 — Glycogen Phosphorylase B;
Domain ID domain_id1ygpA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2000 — Glycogen Phosphorylase B;
Domain ID domain_id1ygpB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2000 — Glycogen Phosphorylase B;
Domain ID domain_id1ygpB02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2000 — Glycogen Phosphorylase B;
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7. Citations (4)