1p89

Substrate-induced Structural Changes to the Isolated N-Terminal Domain of 5-Enolpyruvylshikimate-3-phosphate Synthase

Method: SOLUTION NMR

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

3-phosphoshikimate 1-carboxyvinyltransferase

Escherichia coli

UniProt P0A6D3

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 No other associated polymer Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name AROA_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–216; UniProt 25–240

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.

2. Structure Basics 2. Structure Basics

Entry ID entry_id1p89
Deposition date deposition_date2003-05-06
Structure title titleSubstrate-induced Structural Changes to the Isolated N-Terminal Domain of 5-Enolpyruvylshikimate-3-phosphate Synthase
Keywords keywordsS3P, EPSP synthase, Structure from MOLMOL, Transferase; TRANSFERASE
Experimental Method methodSOLUTION NMR

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.

1p89__assembly_1__model_2

Assembly 1 · Model 2 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1p89__assembly_1__model_2 | I(q)

10-2 10-1 105 106 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1p89__assembly_1__model_2 | 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)16.91 Å
Rg (electron density)15.40 Å
Total Rg16.42 Å
Atom count3275
Residues216
Excluded volume29036 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1p89__assembly_1__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 2 1p89__assembly_1__model_2 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 3 1p89__assembly_1__model_3 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 4 1p89__assembly_1__model_4 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 5 1p89__assembly_1__model_5 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 6 1p89__assembly_1__model_6 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 7 1p89__assembly_1__model_7 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 8 1p89__assembly_1__model_8 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 9 1p89__assembly_1__model_9 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 10 1p89__assembly_1__model_10 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 11 1p89__assembly_1__model_11 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download

4. Crystallography and Experiment 4. Crystallography & Experiment

5. Entities and Polymers Entities & Polymers (1)

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1p89a_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.68 — IF3-like
Superfamily Superfamily superfamilyd.68.2 — EPT/RTPC-like
Family Family familyd.68.2.2 — Enolpyruvate transferase, EPT

CATH v4.4 (1 domains)

Domain ID domain_id1p89A00
Class class3 — Alpha Beta
Architecture architecture65 — Alpha-beta prism
Topology topology10 — UDP-n-acetylglucosamine1-carboxyvinyl-transferase; Chain
Homologous superfamily homologous superfamily10 — Enolpyruvate transferase domain

7. Citations (1)