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4uag

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

Method: X-RAY DIFFRACTION
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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 SULFATE ION × 1 URIDINE-5'-DIPHOSPHATE-N-ACETYLMURAMOYL-L-ALANINE-D-GLUTAMATE × 1 UNKNOWN ATOM OR ION × 8 water × 1 Consistent with protein count

Other States of the Same Protein in the Database

Monomer
1e0d 1eeh 1uag 2jff 2jfg 2jfh 2uag 2uuo 2uup 2vtd 2vte 2wjp

30 assemblies; showing the first 12

Homodimer

None

Homotetramer

None

Other homooligomers

None

Heteromeric or nucleic-acid complex

None

View Construct and Data Evidence
UniProt name MURD_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–437； UniProt 2–438

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_id4uag
Deposition date deposition_date1999-03-09
Structure title titleUDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE
Keywords keywordsLIGASE, PEPTIDOGLYCAN SYNTHESIS, MURD, ADP-FORMING ENZYME; LIGASE
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.

Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 4uag__assembly_1__model_1 monomeric （1） Excluded — —
Exclusion reason： The source record does not identify the atom or ion element unambiguously, so a reliable calculation is not possible.
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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) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd4uaga1
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_idd4uaga2
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_idd4uaga3
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_id4uagA01
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_id4uagA02
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_id4uagA03
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 (3)