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Crystal structure of megavirus udp-glcnac 4,6-dehydratase, 5-epimerase MG534

Analyse Crystal structure of megavirus udp-glcnac 4,6-dehydratase, 5-epimerase MG534 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4TQG
Type: protein
Length: 297 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative dtdp-D-glucose 4 6-dehydratase
UniProt: G5CSR9
Ligands: NDP
Pockets: 3 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative dtdp-D-glucose 4 6-dehydratase	protein	297	41% helix, 22% strand	G5CSR9

Ligands and binding sites

NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	676	0.74	0.80	68	NDP
2	78	0.36	0.76	19	empty
3	51	0.30	0.75	13	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

4TQG · Crystal structure of Megavirus UDP-GlcNAc 4,6-dehydratase, 5-epimerase Mg534 · 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
Every structure of UniProt G5CSR9
Elsewhere: RCSB PDB 4TQG · PDBe 4TQG · UniProt G5CSR9

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