3swd

E. coli MurA in complex with UDP-N-acetylmuramic acid and covalent adduct of PEP with Cys115

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

UDP-N-acetylglucosamine 1-carboxyvinyltransferase

Escherichia coli

UniProt P0A749

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 ;(2R)-2-{[(2R,3R,4R,5S,6R)-3-(acetylamino)-2-{[(S)-{[(R)-{[(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methoxy}(hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl]oxy}-5-hydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-4-yl]oxy}propanoic acid ; × 1 water × 1 Consistent with protein count
10 Protein monomer Monomer Protein 1 ;(2R)-2-{[(2R,3R,4R,5S,6R)-3-(acetylamino)-2-{[(S)-{[(R)-{[(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methoxy}(hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl]oxy}-5-hydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-4-yl]oxy}propanoic acid ; × 1 water × 1 Consistent with protein count
11 Protein monomer Monomer Protein 1 ;(2R)-2-{[(2R,3R,4R,5S,6R)-3-(acetylamino)-2-{[(S)-{[(R)-{[(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methoxy}(hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl]oxy}-5-hydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-4-yl]oxy}propanoic acid ; × 1 water × 1 Consistent with protein count
12 Protein monomer Monomer Protein 1 ;(2R)-2-{[(2R,3R,4R,5S,6R)-3-(acetylamino)-2-{[(S)-{[(R)-{[(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methoxy}(hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl]oxy}-5-hydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-4-yl]oxy}propanoic acid ; × 1 water × 1 Consistent with protein count
13 Protein homooligomer Homooligomer Protein 4 ;(2R)-2-{[(2R,3R,4R,5S,6R)-3-(acetylamino)-2-{[(S)-{[(R)-{[(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methoxy}(hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl]oxy}-5-hydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-4-yl]oxy}propanoic acid ; × 4 water × 4 Consistent with protein count
14 Protein homooligomer Homooligomer Protein 4 ;(2R)-2-{[(2R,3R,4R,5S,6R)-3-(acetylamino)-2-{[(S)-{[(R)-{[(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methoxy}(hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl]oxy}-5-hydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-4-yl]oxy}propanoic acid ; × 4 water × 4 Consistent with protein count
15 Protein homooligomer Homooligomer Protein 4 ;(2R)-2-{[(2R,3R,4R,5S,6R)-3-(acetylamino)-2-{[(S)-{[(R)-{[(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methoxy}(hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl]oxy}-5-hydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-4-yl]oxy}propanoic acid ; × 4 water × 4 Consistent with protein count
2 Protein monomer Monomer Protein 1 ;(2R)-2-{[(2R,3R,4R,5S,6R)-3-(acetylamino)-2-{[(S)-{[(R)-{[(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methoxy}(hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl]oxy}-5-hydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-4-yl]oxy}propanoic acid ; × 1 water × 1 Consistent with protein count
3 Protein monomer Monomer Protein 1 ;(2R)-2-{[(2R,3R,4R,5S,6R)-3-(acetylamino)-2-{[(S)-{[(R)-{[(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methoxy}(hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl]oxy}-5-hydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-4-yl]oxy}propanoic acid ; × 1 water × 1 Consistent with protein count
4 Protein monomer Monomer Protein 1 ;(2R)-2-{[(2R,3R,4R,5S,6R)-3-(acetylamino)-2-{[(S)-{[(R)-{[(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methoxy}(hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl]oxy}-5-hydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-4-yl]oxy}propanoic acid ; × 1 water × 1 Consistent with protein count
5 Protein monomer Monomer Protein 1 ;(2R)-2-{[(2R,3R,4R,5S,6R)-3-(acetylamino)-2-{[(S)-{[(R)-{[(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methoxy}(hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl]oxy}-5-hydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-4-yl]oxy}propanoic acid ; × 1 water × 1 Consistent with protein count
6 Protein monomer Monomer Protein 1 ;(2R)-2-{[(2R,3R,4R,5S,6R)-3-(acetylamino)-2-{[(S)-{[(R)-{[(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methoxy}(hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl]oxy}-5-hydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-4-yl]oxy}propanoic acid ; × 1 water × 1 Consistent with protein count
7 Protein monomer Monomer Protein 1 ;(2R)-2-{[(2R,3R,4R,5S,6R)-3-(acetylamino)-2-{[(S)-{[(R)-{[(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methoxy}(hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl]oxy}-5-hydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-4-yl]oxy}propanoic acid ; × 1 water × 1 Consistent with protein count
8 Protein monomer Monomer Protein 1 ;(2R)-2-{[(2R,3R,4R,5S,6R)-3-(acetylamino)-2-{[(S)-{[(R)-{[(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methoxy}(hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl]oxy}-5-hydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-4-yl]oxy}propanoic acid ; × 1 water × 1 Consistent with protein count
9 Protein monomer Monomer Protein 1 ;(2R)-2-{[(2R,3R,4R,5S,6R)-3-(acetylamino)-2-{[(S)-{[(R)-{[(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methoxy}(hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl]oxy}-5-hydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-4-yl]oxy}propanoic acid ; × 1 water × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name MURA_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–418; UniProt 1–418 Author chain B; PDBConstruct 1–418; UniProt 1–418 Author chain C; PDBConstruct 1–418; UniProt 1–418 Author chain D; PDBConstruct 1–418; UniProt 1–418 Author chain E; PDBConstruct 1–418; UniProt 1–418 Author chain F; PDBConstruct 1–418; UniProt 1–418 Author chain G; PDBConstruct 1–418; UniProt 1–418 Author chain H; PDBConstruct 1–418; UniProt 1–418 Author chain I; PDBConstruct 1–418; UniProt 1–418 Author chain J; PDBConstruct 1–418; UniProt 1–418 Author chain K; PDBConstruct 1–418; UniProt 1–418 Author chain L; PDBConstruct 1–418; UniProt 1–418

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_id3swd
Deposition date deposition_date2011-07-13
Structure title titleE. coli MurA in complex with UDP-N-acetylmuramic acid and covalent adduct of PEP with Cys115
Keywords keywordsMURA, CLOSE ENZYME STATE, CELL WALL, BIOGENESIS/DEGRADATION, 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.

3swd__assembly_11__model_1

Assembly 11 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

3swd__assembly_11__model_1 | I(q)

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

3swd__assembly_11__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)22.56 Å
Rg (electron density)21.54 Å
Total Rg22.28 Å
Atom count3187
Residues416
Excluded volume56878 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 3swd__assembly_1__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 3swd__assembly_2__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
3 1 3swd__assembly_3__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
4 1 3swd__assembly_4__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
5 1 3swd__assembly_5__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
6 1 3swd__assembly_6__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
7 1 3swd__assembly_7__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
8 1 3swd__assembly_8__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
9 1 3swd__assembly_9__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
10 1 3swd__assembly_10__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
11 1 3swd__assembly_11__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
12 1 3swd__assembly_12__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
13 1 3swd__assembly_13__model_1 tetrameric (4) Success 4.1.3-1-20251215 (887e7ef) View Download
14 1 3swd__assembly_14__model_1 tetrameric (4) Success 4.1.3-1-20251215 (887e7ef) View Download
15 1 3swd__assembly_15__model_1 tetrameric (4) 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 (3)

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6. Fold Classification (SCOP + CATH) 36 domains

SCOP 2.08 (12 domains)

Domain ID domain_idd3swda_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.68 — IF3-like
Superfamily Superfamily superfamilyd.68.2 — EPT/RTPC-like
Family Family familyd.68.2.2 — Enolpyruvate transferase, EPT
Domain ID domain_idd3swdb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.68 — IF3-like
Superfamily Superfamily superfamilyd.68.2 — EPT/RTPC-like
Family Family familyd.68.2.2 — Enolpyruvate transferase, EPT
Domain ID domain_idd3swdc_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.68 — IF3-like
Superfamily Superfamily superfamilyd.68.2 — EPT/RTPC-like
Family Family familyd.68.2.2 — Enolpyruvate transferase, EPT
Domain ID domain_idd3swdd_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.68 — IF3-like
Superfamily Superfamily superfamilyd.68.2 — EPT/RTPC-like
Family Family familyd.68.2.2 — Enolpyruvate transferase, EPT
Domain ID domain_idd3swde_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.68 — IF3-like
Superfamily Superfamily superfamilyd.68.2 — EPT/RTPC-like
Family Family familyd.68.2.2 — Enolpyruvate transferase, EPT
Domain ID domain_idd3swdf_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.68 — IF3-like
Superfamily Superfamily superfamilyd.68.2 — EPT/RTPC-like
Family Family familyd.68.2.2 — Enolpyruvate transferase, EPT
Domain ID domain_idd3swdg_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.68 — IF3-like
Superfamily Superfamily superfamilyd.68.2 — EPT/RTPC-like
Family Family familyd.68.2.2 — Enolpyruvate transferase, EPT
Domain ID domain_idd3swdh_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.68 — IF3-like
Superfamily Superfamily superfamilyd.68.2 — EPT/RTPC-like
Family Family familyd.68.2.2 — Enolpyruvate transferase, EPT
Domain ID domain_idd3swdi_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.68 — IF3-like
Superfamily Superfamily superfamilyd.68.2 — EPT/RTPC-like
Family Family familyd.68.2.2 — Enolpyruvate transferase, EPT
Domain ID domain_idd3swdj_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.68 — IF3-like
Superfamily Superfamily superfamilyd.68.2 — EPT/RTPC-like
Family Family familyd.68.2.2 — Enolpyruvate transferase, EPT
Domain ID domain_idd3swdk_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.68 — IF3-like
Superfamily Superfamily superfamilyd.68.2 — EPT/RTPC-like
Family Family familyd.68.2.2 — Enolpyruvate transferase, EPT
Domain ID domain_idd3swdl_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.68 — IF3-like
Superfamily Superfamily superfamilyd.68.2 — EPT/RTPC-like
Family Family familyd.68.2.2 — Enolpyruvate transferase, EPT

CATH v4.4 (24 domains)

Domain ID domain_id3swdA01
Class class3 — Alpha Beta
Architecture architecture65 — Alpha-beta prism
Topology topology10 — UDP-n-acetylglucosamine1-carboxyvinyl-transferase; Chain
Homologous superfamily homologous superfamily10 — Enolpyruvate transferase domain
Domain ID domain_id3swdA02
Class class3 — Alpha Beta
Architecture architecture65 — Alpha-beta prism
Topology topology10 — UDP-n-acetylglucosamine1-carboxyvinyl-transferase; Chain
Homologous superfamily homologous superfamily10 — Enolpyruvate transferase domain
Domain ID domain_id3swdB01
Class class3 — Alpha Beta
Architecture architecture65 — Alpha-beta prism
Topology topology10 — UDP-n-acetylglucosamine1-carboxyvinyl-transferase; Chain
Homologous superfamily homologous superfamily10 — Enolpyruvate transferase domain
Domain ID domain_id3swdB02
Class class3 — Alpha Beta
Architecture architecture65 — Alpha-beta prism
Topology topology10 — UDP-n-acetylglucosamine1-carboxyvinyl-transferase; Chain
Homologous superfamily homologous superfamily10 — Enolpyruvate transferase domain
Domain ID domain_id3swdC01
Class class3 — Alpha Beta
Architecture architecture65 — Alpha-beta prism
Topology topology10 — UDP-n-acetylglucosamine1-carboxyvinyl-transferase; Chain
Homologous superfamily homologous superfamily10 — Enolpyruvate transferase domain
Domain ID domain_id3swdC02
Class class3 — Alpha Beta
Architecture architecture65 — Alpha-beta prism
Topology topology10 — UDP-n-acetylglucosamine1-carboxyvinyl-transferase; Chain
Homologous superfamily homologous superfamily10 — Enolpyruvate transferase domain
Domain ID domain_id3swdD01
Class class3 — Alpha Beta
Architecture architecture65 — Alpha-beta prism
Topology topology10 — UDP-n-acetylglucosamine1-carboxyvinyl-transferase; Chain
Homologous superfamily homologous superfamily10 — Enolpyruvate transferase domain
Domain ID domain_id3swdD02
Class class3 — Alpha Beta
Architecture architecture65 — Alpha-beta prism
Topology topology10 — UDP-n-acetylglucosamine1-carboxyvinyl-transferase; Chain
Homologous superfamily homologous superfamily10 — Enolpyruvate transferase domain
Domain ID domain_id3swdE01
Class class3 — Alpha Beta
Architecture architecture65 — Alpha-beta prism
Topology topology10 — UDP-n-acetylglucosamine1-carboxyvinyl-transferase; Chain
Homologous superfamily homologous superfamily10 — Enolpyruvate transferase domain
Domain ID domain_id3swdE02
Class class3 — Alpha Beta
Architecture architecture65 — Alpha-beta prism
Topology topology10 — UDP-n-acetylglucosamine1-carboxyvinyl-transferase; Chain
Homologous superfamily homologous superfamily10 — Enolpyruvate transferase domain
Domain ID domain_id3swdF01
Class class3 — Alpha Beta
Architecture architecture65 — Alpha-beta prism
Topology topology10 — UDP-n-acetylglucosamine1-carboxyvinyl-transferase; Chain
Homologous superfamily homologous superfamily10 — Enolpyruvate transferase domain
Domain ID domain_id3swdF02
Class class3 — Alpha Beta
Architecture architecture65 — Alpha-beta prism
Topology topology10 — UDP-n-acetylglucosamine1-carboxyvinyl-transferase; Chain
Homologous superfamily homologous superfamily10 — Enolpyruvate transferase domain
Domain ID domain_id3swdG01
Class class3 — Alpha Beta
Architecture architecture65 — Alpha-beta prism
Topology topology10 — UDP-n-acetylglucosamine1-carboxyvinyl-transferase; Chain
Homologous superfamily homologous superfamily10 — Enolpyruvate transferase domain
Domain ID domain_id3swdG02
Class class3 — Alpha Beta
Architecture architecture65 — Alpha-beta prism
Topology topology10 — UDP-n-acetylglucosamine1-carboxyvinyl-transferase; Chain
Homologous superfamily homologous superfamily10 — Enolpyruvate transferase domain
Domain ID domain_id3swdH01
Class class3 — Alpha Beta
Architecture architecture65 — Alpha-beta prism
Topology topology10 — UDP-n-acetylglucosamine1-carboxyvinyl-transferase; Chain
Homologous superfamily homologous superfamily10 — Enolpyruvate transferase domain
Domain ID domain_id3swdH02
Class class3 — Alpha Beta
Architecture architecture65 — Alpha-beta prism
Topology topology10 — UDP-n-acetylglucosamine1-carboxyvinyl-transferase; Chain
Homologous superfamily homologous superfamily10 — Enolpyruvate transferase domain
Domain ID domain_id3swdI01
Class class3 — Alpha Beta
Architecture architecture65 — Alpha-beta prism
Topology topology10 — UDP-n-acetylglucosamine1-carboxyvinyl-transferase; Chain
Homologous superfamily homologous superfamily10 — Enolpyruvate transferase domain
Domain ID domain_id3swdI02
Class class3 — Alpha Beta
Architecture architecture65 — Alpha-beta prism
Topology topology10 — UDP-n-acetylglucosamine1-carboxyvinyl-transferase; Chain
Homologous superfamily homologous superfamily10 — Enolpyruvate transferase domain
Domain ID domain_id3swdJ01
Class class3 — Alpha Beta
Architecture architecture65 — Alpha-beta prism
Topology topology10 — UDP-n-acetylglucosamine1-carboxyvinyl-transferase; Chain
Homologous superfamily homologous superfamily10 — Enolpyruvate transferase domain
Domain ID domain_id3swdJ02
Class class3 — Alpha Beta
Architecture architecture65 — Alpha-beta prism
Topology topology10 — UDP-n-acetylglucosamine1-carboxyvinyl-transferase; Chain
Homologous superfamily homologous superfamily10 — Enolpyruvate transferase domain
Domain ID domain_id3swdK01
Class class3 — Alpha Beta
Architecture architecture65 — Alpha-beta prism
Topology topology10 — UDP-n-acetylglucosamine1-carboxyvinyl-transferase; Chain
Homologous superfamily homologous superfamily10 — Enolpyruvate transferase domain
Domain ID domain_id3swdK02
Class class3 — Alpha Beta
Architecture architecture65 — Alpha-beta prism
Topology topology10 — UDP-n-acetylglucosamine1-carboxyvinyl-transferase; Chain
Homologous superfamily homologous superfamily10 — Enolpyruvate transferase domain
Domain ID domain_id3swdL01
Class class3 — Alpha Beta
Architecture architecture65 — Alpha-beta prism
Topology topology10 — UDP-n-acetylglucosamine1-carboxyvinyl-transferase; Chain
Homologous superfamily homologous superfamily10 — Enolpyruvate transferase domain
Domain ID domain_id3swdL02
Class class3 — Alpha Beta
Architecture architecture65 — Alpha-beta prism
Topology topology10 — UDP-n-acetylglucosamine1-carboxyvinyl-transferase; Chain
Homologous superfamily homologous superfamily10 — Enolpyruvate transferase domain
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7. Citations (2)