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Structure of mura liganded with the extrinsic fluorescence probe ans

Analyse Structure of mura liganded with the extrinsic fluorescence probe ans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1EYN
Type
protein
Length
419 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Udp-N-acetylglucosamine 1-carboxyvinyltransferase
EC
2.5.1.7
UniProt
P33038
Ligands
2AN
Pockets
2 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUdp-N-acetylglucosamine 1-carboxyvinyltransferase (EC 2.5.1.7)protein41934% helix, 27% strandP33038

Ligands and binding sites

  • 2AN · 8-anilino-1-naphthalene sulfonate · ligand · chains A
  • GOL · Glycerol · additive · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16990.690.77582AN, GOL
2750.360.7717empty

Modifications

Observed in the structure: 1 modified (nonstandard).

Compared structures

  • 1EYN · Structure of mura liganded with the extrinsic fluorescence probe ANS · the same entry in another collection · chain A against A, TM-score 1.00
  • P33038 · AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine 1-carboxyvinyltransferase… · a predicted model of the same protein · chain A against A, TM-score 0.95

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