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Crystal structure analysis of the methyltransferase domain of bacterial-AVHEN1-C

Analyse Crystal structure analysis of the methyltransferase domain of bacterial-AVHEN1-C in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3JWH
Type: protein
Length: 379 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: HEN1
UniProt: Q3MCR9
Ligands: SAH
Pockets: 3 · best druggability 0.46

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	HEN1	protein	191	41% helix, 23% strand	Q3MCR9
B	HEN1	protein	188	41% helix, 23% strand	Q3MCR9

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

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	162	0.46	0.76	25	SAH
2	141	0.43	0.76	24	SAH
3	69	0.29	0.74	14	empty

Interfaces

1 interface between chains.

A–B · 161 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

3JWH · Crystal structure analysis of the methyltransferase domain of bacterial-AvHen1-C · the same entry in another collection · chain B against B, 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 Q3MCR9
Elsewhere: RCSB PDB 3JWH · PDBe 3JWH · UniProt Q3MCR9

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