MolNFT v1 · #114431 · protein

Crystal structure of SAM-dependent methyltransferase from bacteroides fragilis in complex with S-adenosyl-L-homocysteine

5BP9 · Putative methyltransferase protein: “Crystal structure of SAM-dependent methyltransferase from bacteroides fragilis in complex with…”. X-ray diffraction, 2 ligands (ETE, SAH), 1 pocket (best druggability 0.77). MolNFT v1 #114431 on…

PDB: 5BP9
Type: protein
Length: 237 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative methyltransferase protein
UniProt: Q5LFK0
Ligands: ETE, SAH
Pockets: 1 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative methyltransferase protein	protein	237	33% helix, 29% strand	Q5LFK0

Ligands and binding sites

ETE · 2-{2-[2-2-(methoxy-ethoxy)-ethoxy]-ethoxy}-ethanol · ligand · chains A
SAH · S-adenosyl-L-homocysteine · ligand · chains A
PG4 · Tetraethylene glycol · additive · 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	805	0.77	0.81	76	ETE, SAH

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

5BP9 · Crystal structure of SAM-dependent methyltransferase from Bacteroides fragilis in 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 Q5LFK0
Elsewhere: RCSB PDB 5BP9 · PDBe 5BP9 · UniProt Q5LFK0

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