1eeh

UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE

Method: X-RAY DIFFRACTION

1. Protein Identity and Related Structures Protein Identity & Related Structures

UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE

Escherichia coli

UniProt P14900

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 URIDINE-5'-DIPHOSPHATE-N-ACETYLMURAMOYL-L-ALANINE × 1 water × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name MURD_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–437; UniProt 1–437

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.

2. Structure Basics 2. Structure Basics

Entry ID entry_id1eeh
Deposition date deposition_date2000-01-31
Structure title titleUDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE
Keywords keywordsLIGASE, PEPTIDOGLYCAN SYNTHESIS, MURD, ADP-FORMING ENZYME; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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.

1eeh__assembly_1__model_1

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

Download this curve (.dat)

1eeh__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.

1eeh__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)23.96 Å
Rg (electron density)22.92 Å
Total Rg23.69 Å
Atom count3286
Residues431
Excluded volume58369 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1eeh__assembly_1__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download

4. Crystallography and Experiment 4. Crystallography & Experiment

5. Entities and Polymers Entities & Polymers (3)

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1eeha1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.5 — MurCD N-terminal domain
Superfamily Superfamily superfamilyc.5.1 — MurCD N-terminal domain
Family Family familyc.5.1.1 — MurCD N-terminal domain
Domain ID domain_idd1eeha2
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.59.1.1 — MurCDEF C-terminal domain
Domain ID domain_idd1eeha3
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.72.2.1 — MurCDEF

CATH v4.4 (3 domains)

Domain ID domain_id1eehA01
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_id1eehA02
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
Domain ID domain_id1eehA03
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

7. Citations (3)