4g3p

Crystal structure of GlmU from Mycobacterium tuberculosis Snapshot 3

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

Bifunctional protein GlmU

Mycobacterium tuberculosis

UniProt P96382

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 3 PYROPHOSPHATE 2- × 3 MAGNESIUM ION × 6 COBALT (II) ION × 6 URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE × 3 water × 3 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name GLMU_MYCTU
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 7–501; UniProt 1–495

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_id4g3p
Deposition date deposition_date2012-07-15
Structure title titleCrystal structure of GlmU from Mycobacterium tuberculosis Snapshot 3
Keywords keywords;ACETYLTRANSFERASE, BIFUNCTIONAL, PYROPHOSPHORYLASE, ROSSMANN-LIKE FOLD, LEFT-HANDED-BETA-HELIX, CELL SHAPE, CELL WALL BIOGENESIS/DEGRADATION, METAL-BINDING, MULTIFUNCTIONAL ENZYME, NUCLEOTIDYLTRANSFERASE, PEPTIDOGLYCAN SYNTHESIS, 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.

4g3p__assembly_1__model_1

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

Download this curve (.dat)

4g3p__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.

4g3p__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)36.93 Å
Rg (electron density)36.20 Å
Total Rg36.55 Å
Atom count10274
Residues1386
Excluded volume180850 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 4g3p__assembly_1__model_1 trimeric (3) 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 (6)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4g3pa1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.68 — Nucleotide-diphospho-sugar transferases
Superfamily Superfamily superfamilyc.68.1 — Nucleotide-diphospho-sugar transferases
Family Family familyc.68.1.0 — automated matches
Domain ID domain_idd4g3pa2
Class classb — All beta proteins
Fold Fold foldb.81 — Single-stranded left-handed beta-helix
Superfamily Superfamily superfamilyb.81.1 — Trimeric LpxA-like enzymes
Family Family familyb.81.1.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id4g3pA01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology550 — Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A
Homologous superfamily homologous superfamily10 — Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A
Domain ID domain_id4g3pA02
Class class2 — Mainly Beta
Architecture architecture160 — 3 Solenoid
Topology topology10 — UDP N-Acetylglucosamine Acyltransferase; domain 1
Homologous superfamily homologous superfamily10 — Hexapeptide repeat proteins
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7. Citations (1)