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Crystal structure of C-terminal half of bacterial HEN1

Analyse Crystal structure of C-terminal half of bacterial HEN1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4DQZ
Type
protein
Length
342 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Methyltransferase type 12
UniProt
A3DJ37
Pockets
5 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BMethyltransferase type 12protein17136% helix, 33% strandA3DJ37

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11850.530.7929empty
21380.490.7921empty
31070.440.7820empty
4930.400.7715empty
5500.310.7612empty

Interfaces

1 interface between chains.

  • A–B · 1029 Ų buried · 15 hydrogen bonds · protein-protein

Compared structures

  • 4DQZ · Crystal Structure of C-terminal Half of Bacterial Hen1 · the same entry in another collection · chain A against A, TM-score 1.00

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