1xff

Glutaminase domain of glucosamine 6-phosphate synthase complexed with glutamate

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

Glucosamine--fructose-6-phosphate aminotransferase [isomerizing]

Escherichia coli

UniProt P17169

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 2 SODIUM ION × 2 ACETATE ION × 1 GLUTAMIC ACID × 2 water × 2 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name GLMS_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–240; UniProt 1–240 Author chain B; PDBConstruct 1–240; UniProt 1–240

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id1xff
Deposition date deposition_date2004-09-14
Structure title titleGlutaminase domain of glucosamine 6-phosphate synthase complexed with glutamate
Keywords keywordsCOMPLEX (TRANSFERASE-INHIBITOR); GLUTAMINE AMIDOTRANSFERASE, TRANSFERASE; TRANSFERASE
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.

1xff__assembly_1__model_1

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

Download this curve (.dat)

1xff__assembly_1__model_1 | I(q)

10-2 10-1 105 106 107 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1xff__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)26.60 Å
Rg (electron density)25.99 Å
Total Rg26.51 Å
Atom count3721
Residues477
Excluded volume65688 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1xff__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 (5)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1xffa_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.153 — Ntn hydrolase-like
Superfamily Superfamily superfamilyd.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family familyd.153.1.1 — Class II glutamine amidotransferases
Domain ID domain_idd1xffb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.153 — Ntn hydrolase-like
Superfamily Superfamily superfamilyd.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family familyd.153.1.1 — Class II glutamine amidotransferases

CATH v4.4 (2 domains)

Domain ID domain_id1xffA00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id1xffB00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
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7. Citations (3)