3dr3

Structure of IDP00107, a potential N-acetyl-gamma-glutamylphosphate reductase from Shigella flexneri

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

N-acetyl-gamma-glutamyl-phosphate reductase

Shigella flexneri

UniProt P59310

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 4 SODIUM ION × 8 D-MALATE × 4 water × 4 Consistent with protein count
2 Protein homooligomer Homooligomer Protein 2 SODIUM ION × 4 D-MALATE × 2 water × 2 Consistent with protein count
3 Protein homooligomer Homooligomer Protein 2 SODIUM ION × 4 D-MALATE × 2 water × 2 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name ARGC_SHIFL
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–337; UniProt 1–334

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_id3dr3
Deposition date deposition_date2008-07-10
Structure title titleStructure of IDP00107, a potential N-acetyl-gamma-glutamylphosphate reductase from Shigella flexneri
Keywords keywords;CSGID target, argC, Shigella flexneri, essential gene, Amino-acid biosynthesis, Arginine biosynthesis, Cytoplasm, NADP, Oxidoreductase. FUNDED BY THE NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES OF NIH CONTRACT NUMBER HHSN272200700058C, Structural Genomics, Center for Structural Genomics of Infectious Diseases, OXIDOREDUCTASE ;; OXIDOREDUCTASE
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.

3dr3__assembly_1__model_1

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

Download this curve (.dat)

3dr3__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.

3dr3__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)33.07 Å
Rg (electron density)31.85 Å
Total Rg32.54 Å
Atom count10192
Residues1340
Excluded volume182280 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 3dr3__assembly_1__model_1 tetrameric (4) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 3dr3__assembly_2__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
3 1 3dr3__assembly_3__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 (4)

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6. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id3dr3A01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily720 — NAD(P)-binding Rossmann-like Domain
Domain ID domain_id3dr3A02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology360 — Dihydrodipicolinate Reductase; domain 2
Homologous superfamily homologous superfamily10 — Dihydrodipicolinate Reductase; domain 2
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7. Citations (2)