2pts

Crystal structure of wild type Escherichia coli adenylosuccinate lyase

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

Adenylosuccinate lyase

Escherichia coli

UniProt P0AB89

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 4 water × 4 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name PUR8_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–456; UniProt 1–456

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_id2pts
Deposition date deposition_date2007-05-08
Structure title titleCrystal structure of wild type Escherichia coli adenylosuccinate lyase
Keywords keywordsadenylosuccinate lyase, wild-type-selenomethionine substituted, LYASE; LYASE
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.

2pts__assembly_1__model_1

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

Download this curve (.dat)

2pts__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.

2pts__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)36.70 Å
Rg (electron density)36.14 Å
Total Rg36.63 Å
Atom count14056
Residues1752
Excluded volume250470 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 2pts__assembly_1__model_1 tetrameric (4) 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 (2)

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6. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2ptsa1
Class classa — All alpha proteins
Fold Fold folda.127 — L-aspartase-like
Superfamily Superfamily superfamilya.127.1 — L-aspartase-like
Family Family familya.127.1.0 — automated matches
Domain ID domain_idd2ptsa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (3 domains)

Domain ID domain_id2ptsA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology275 — Fumarase C; Chain B, domain 1
Homologous superfamily homologous superfamily10 — Fumarase/aspartase (N-terminal domain)
Domain ID domain_id2ptsA02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology200 — Fumarase C; Chain A, domain 2
Homologous superfamily homologous superfamily10 — Fumarase/aspartase (Central domain)
Domain ID domain_id2ptsA03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology40 — Ribonucleotide Reductase Protein R1; domain 1
Homologous superfamily homologous superfamily30 — Fumarase/aspartase (C-terminal domain)
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7. Citations (1)