GL1X · GenesisL1 explorer

Research workbench

Crystal structure of a predicted O-methyltransferase, protein ATU636 from agrobacterium tumefaciens.

Analyse Crystal structure of a predicted O-methyltransferase, protein ATU636 from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2OZV
Type
protein
Length
418 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hypothetical protein ATU0636
UniProt
Q8UHP4
Pockets
3 · best druggability 0.40

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHypothetical protein ATU0636protein20832% helix, 27% strandQ8UHP4
BHypothetical protein ATU0636protein21033% helix, 28% strandQ8UHP4

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11450.400.7329empty
2890.350.7518empty
3600.340.7716empty

Interfaces

1 interface between chains.

  • A–B · 806 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 modified (engineered).

Compared structures

  • 2OZV · Crystal structure of a predicted O-methyltransferase, protein Atu636 from Agrobacterium… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.