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Crystal structure of bergaptol O-methyltransferase complex

Analyse Crystal structure of bergaptol O-methyltransferase complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5XOH
Type: protein
Length: 348 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bergaptol O-methyltransferase
EC: 2.1.1.69
UniProt: A0A166U5H3
Ligands: SAH, 8B6
Pockets: 4 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bergaptol O-methyltransferase (EC 2.1.1.69)	protein	348	50% helix, 13% strand	A0A166U5H3

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · chains A
8B6 · 4-oxidanylfuro[3,2-g]chromen-7-one · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	298	0.81	0.92	46	SAH, 8B6
2	641	0.69	0.77	34	empty
3	165	0.65	0.85	27	empty
4	65	0.29	0.74	19	empty

Compared structures

5XOH · Crystal structure of bergaptol o-methyltransferase complex · 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 A0A166U5H3
Elsewhere: RCSB PDB 5XOH · PDBe 5XOH · UniProt A0A166U5H3

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