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Crystal structure of a murb family ep-udp-N-acetylglucosamine reductase

Analyse Crystal structure of a murb family ep-udp-N-acetylglucosamine reductase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4PYT
Type: protein
Length: 302 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Udp-N-acetylenolpyruvoylglucosamine reductase
EC: 1.3.1.98
Ligands: FAD, MG, CL
Pockets: 1 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Udp-N-acetylenolpyruvoylglucosamine reductase (EC 1.3.1.98)	protein	302	33% helix, 28% strand	—

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A
MG · Magnesium ion · metal · 3 copies · chains A
CL · Chloride ion · ion · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	640	0.76	0.82	67	FAD

Compared structures

4PYT · Crystal structure of a MurB family EP-UDP-N-acetylglucosamine reductase · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 4PYT · PDBe 4PYT

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