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Crystal structure of burkholderia glumae toxa with bound S- adenosylhomocysteine (sah) and 1-demethyltoxoflavin

Analyse Crystal structure of burkholderia glumae toxa with bound S… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5JE5
Type: protein
Length: 243 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methyl transferase
UniProt: Q9LBJ0
Ligands: SAH, AZ9
Pockets: 1 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Methyl transferase	protein	243	39% helix, 28% strand	Q9LBJ0

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · chains A
AZ9 · 6-methylpyrimido[5,4-e][1,2,4]triazine-5,7(6H,8H)-dione · ligand · 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	324	0.76	0.87	48	SAH, AZ9

Compared structures

5JE5 · Crystal structure of Burkholderia glumae ToxA with bound S-adenosylhomocysteine (SAH) and… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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Every structure of UniProt Q9LBJ0
Elsewhere: RCSB PDB 5JE5 · PDBe 5JE5 · UniProt Q9LBJ0

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