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Crystal structure of methyltransferase with LIGAND(SAH)

Analyse Crystal structure of methyltransferase with LIGAND(SAH) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2CX8
Type: protein
Length: 398 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methyl transferase
UniProt: Q5SKI6
Ligands: SAH
Pockets: 4 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Methyl transferase	protein	225	31% helix, 24% strand	Q5SKI6
B	Methyl transferase	protein	173	35% helix, 17% strand	Q5SKI6

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · 2 copies · chains A, B

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	567	0.71	0.80	62	SAH
2	155	0.58	0.83	20	empty
3	162	0.58	0.82	29	SAH
4	52	0.32	0.77	13	empty

Interfaces

1 interface between chains.

A–B · 1859 Å² buried · 48 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (engineered).

Compared structures

2CX8 · Crystal structure of methyltransferase with ligand(SAH) · 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 Q5SKI6
Elsewhere: RCSB PDB 2CX8 · PDBe 2CX8 · UniProt Q5SKI6

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