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Crystal structure of catalytic domain of uggt (udp-glucose-bound form) from thermomyces dupontii

Analyse Crystal structure of catalytic domain of uggt (udp-glucose-bound form) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5H18
Type: protein
Length: 272 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uggt
Ligands: UPG, CA
Pockets: 3 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uggt	protein	272	46% helix, 15% strand	—

Ligands and binding sites

UPG · Uridine-5'-diphosphate-glucose · ligand · chains A
CA · Calcium ion · metal · chains A
GOL · Glycerol · additive · 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	323	0.63	0.79	30	UPG
2	123	0.42	0.76	17	empty
3	51	0.35	0.79	13	empty

Modifications

Observed in the structure: 10 modified, 2 disulfide (engineered, disulfide).

Compared structures

5H18 · Crystal structure of catalytic domain of UGGT (UDP-glucose-bound form) from Thermomyces… · 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 5H18 · PDBe 5H18

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