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1fgs

FOLYLPOLYGLUTAMATE SYNTHETASE FROM LACTOBACILLUS CASEI

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

FOLYLPOLYGLUTAMATE SYNTHETASE

Lactobacillus casei

UniProt P15925

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 MAGNESIUM ION × 1 PYROPHOSPHATE 2- × 1 water × 1 Consistent with protein count

Other States of the Same Protein in the Database

Monomer
1fgs 1jbv 1jbw 2gc5 2gc6 2gca 2gcb

7 assemblies

Homodimer

None

Homotetramer

None

Other homooligomers

None

Heteromeric or nucleic-acid complex

None

View Construct and Data Evidence
UniProt name FOLC_LACCA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–428； UniProt 1–428

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_id1fgs
Deposition date deposition_date1998-04-29
Structure title titleFOLYLPOLYGLUTAMATE SYNTHETASE FROM LACTOBACILLUS CASEI
Keywords keywordsSYNTHETASE, LIGASE; SYNTHETASE
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.

1fgs__assembly_1__model_1

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

Download this curve (.dat)

1fgs__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.

1fgs__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）23.01 Å
Rg (electron density)21.95 Å
Total Rg22.81 Å
Atom count2998
Residues393
Excluded volume53523 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1fgs__assembly_1__model_1 monomeric （1） 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) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1fgsa1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.59 — MurD-like peptide ligases, peptide-binding domain
Superfamily Superfamily superfamilyc.59.1 — MurD-like peptide ligases, peptide-binding domain
Family Family familyc.59.1.2 — Folylpolyglutamate synthetase, C-terminal domain
Domain ID domain_idd1fgsa2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.72 — Ribokinase-like
Superfamily Superfamily superfamilyc.72.2 — MurD-like peptide ligases, catalytic domain
Family Family familyc.72.2.2 — Folylpolyglutamate synthetase

CATH v4.4 (2 domains)

Domain ID domain_id1fgsA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1190 — UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase
Homologous superfamily homologous superfamily10 — Mur-like, catalytic domain
Domain ID domain_id1fgsA02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology190 — Protein-Tyrosine Phosphatase; Chain A
Homologous superfamily homologous superfamily20 — Mur ligase, C-terminal domain
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7. Citations (1)