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Crystal structure of putative nucleotide-diphospho-sugar transferase (YP_389115.1) from desulfovibrio desulfuricans G20 at 1.90 a resolution

Analyse Crystal structure of putative nucleotide-diphospho-sugar transferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3CGX
Type: protein
Length: 231 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative nucleotide-diphospho-sugar transferase
UniProt: Q30Y26
Pockets: 3 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative nucleotide-diphospho-sugar transferase	protein	231	44% helix, 17% strand	Q30Y26

Ligands and binding sites

IMD · Imidazole · 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	380	0.63	0.78	37	IMD
2	99	0.45	0.79	18	empty
3	51	0.35	0.79	17	empty

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

3CGX · Crystal structure of putative nucleotide-diphospho-sugar transferase (YP_389115.1) from… · 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 Q30Y26
Elsewhere: RCSB PDB 3CGX · PDBe 3CGX · UniProt Q30Y26

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